An enzyme of the hydrolase class that catalyzes the reaction of triacylglycerol and water to yield diacylglycerol and a fatty acid anion. It is produced by glands on the tongue and by the pancreas and initiates the digestion of dietary fats. (From Dorland, 27th ed) EC 3.1.1.3.
An enzyme of the hydrolase class that catalyzes the reaction of triacylglycerol and water to yield diacylglycerol and a fatty acid anion. The enzyme hydrolyzes triacylglycerols in chylomicrons, very-low-density lipoproteins, low-density lipoproteins, and diacylglycerols. It occurs on capillary endothelial surfaces, especially in mammary, muscle, and adipose tissue. Genetic deficiency of the enzyme causes familial hyperlipoproteinemia Type I. (Dorland, 27th ed) EC 3.1.1.34.
An enzyme that catalyzes the hydrolysis of glycerol monoesters of long-chain fatty acids EC 3.1.1.23.
An enzyme that catalyzes the hydrolysis of CHOLESTEROL ESTERS and some other sterol esters, to liberate cholesterol plus a fatty acid anion.
Colipase I and II, consisting of 94-95 and 84-85 amino acid residues, respectively, have been isolated from porcine pancreas. Their role is to prevent the inhibitory effect of bile salts on the lipase-catalyzed intraduodenal hydrolysis of dietary long-chain triglycerides.
The metabolic process of breaking down LIPIDS to release FREE FATTY ACIDS, the major oxidative fuel for the body. Lipolysis may involve dietary lipids in the DIGESTIVE TRACT, circulating lipids in the BLOOD, and stored lipids in the ADIPOSE TISSUE or the LIVER. A number of enzymes are involved in such lipid hydrolysis, such as LIPASE and LIPOPROTEIN LIPASE from various tissues.
(Z)-9-Octadecenoic acid 1,2,3-propanetriyl ester.
Triglycerides are the most common type of fat in the body, stored in fat cells and used as energy; they are measured in blood tests to assess heart disease risk, with high levels often resulting from dietary habits, obesity, physical inactivity, smoking, and alcohol consumption.
A genus of zygomycetous fungi of the family Mucoraceae, order MUCORALES, a common saprophyte and facultative parasite of mature fruits and vegetables. It may cause cerebral mycoses in diabetes and cutaneous infection in severely burned patients.
A mitosporic Saccharomycetales fungal genus, various species of which have been isolated from pulmonary lesions. Teleomorphs include Dipodascus and Galactomyces.
An inherited condition due to a deficiency of either LIPOPROTEIN LIPASE or APOLIPOPROTEIN C-II (a lipase-activating protein). The lack of lipase activities results in inability to remove CHYLOMICRONS and TRIGLYCERIDES from the blood which has a creamy top layer after standing.
A nodular organ in the ABDOMEN that contains a mixture of ENDOCRINE GLANDS and EXOCRINE GLANDS. The small endocrine portion consists of the ISLETS OF LANGERHANS secreting a number of hormones into the blood stream. The large exocrine portion (EXOCRINE PANCREAS) is a compound acinar gland that secretes several digestive enzymes into the pancreatic ductal system that empties into the DUODENUM.
Enzymes which catalyze the hydrolysis of carboxylic acid esters with the formation of an alcohol and a carboxylic acid anion.
A 9-kDa protein component of VERY-LOW-DENSITY LIPOPROTEINS. It contains a cofactor for LIPOPROTEIN LIPASE and activates several triacylglycerol lipases. The association of Apo C-II with plasma CHYLOMICRONS; VLDL, and HIGH-DENSITY LIPOPROTEINS is reversible and changes rapidly as a function of triglyceride metabolism. Clinically, Apo C-II deficiency is similar to lipoprotein lipase deficiency (HYPERLIPOPROTEINEMIA TYPE I) and is therefore called hyperlipoproteinemia type IB.
A highly acidic mucopolysaccharide formed of equal parts of sulfated D-glucosamine and D-glucuronic acid with sulfaminic bridges. The molecular weight ranges from six to twenty thousand. Heparin occurs in and is obtained from liver, lung, mast cells, etc., of vertebrates. Its function is unknown, but it is used to prevent blood clotting in vivo and vitro, in the form of many different salts.
GLYCEROL esterified with FATTY ACIDS.
A class of lipoproteins that carry dietary CHOLESTEROL and TRIGLYCERIDES from the SMALL INTESTINE to the tissues. Their density (0.93-1.006 g/ml) is the same as that of VERY-LOW-DENSITY LIPOPROTEINS.
Specialized connective tissue composed of fat cells (ADIPOCYTES). It is the site of stored FATS, usually in the form of TRIGLYCERIDES. In mammals, there are two types of adipose tissue, the WHITE FAT and the BROWN FAT. Their relative distributions vary in different species with most adipose tissue being white.
The process of cleaving a chemical compound by the addition of a molecule of water.
Enzymes which are immobilized on or in a variety of water-soluble or water-insoluble matrices with little or no loss of their catalytic activity. Since they can be reused continuously, immobilized enzymes have found wide application in the industrial, medical and research fields.
Carboxylesterase is a serine-dependent esterase with wide substrate specificity. The enzyme is involved in the detoxification of XENOBIOTICS and the activation of ester and of amide PRODRUGS.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
A group of amylolytic enzymes that cleave starch, glycogen, and related alpha-1,4-glucans. (Stedman, 25th ed) EC 3.2.1.-.
Physiological processes in biosynthesis (anabolism) and degradation (catabolism) of LIPIDS.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
A group of apolipoproteins that can readily exchange among the various classes of lipoproteins (HDL; VLDL; CHYLOMICRONS). After lipolysis of TRIGLYCERIDES on VLDL and chylomicrons, Apo-C proteins are normally transferred to HDL. The subtypes can modulate remnant binding to receptors, LECITHIN CHOLESTEROL ACYLTRANSFERASE, or LIPOPROTEIN LIPASE.
Lipid-protein complexes involved in the transportation and metabolism of lipids in the body. They are spherical particles consisting of a hydrophobic core of TRIGLYCERIDES and CHOLESTEROL ESTERS surrounded by a layer of hydrophilic free CHOLESTEROL; PHOSPHOLIPIDS; and APOLIPOPROTEINS. Lipoproteins are classified by their varying buoyant density and sizes.
A class of lipoproteins of very light (0.93-1.006 g/ml) large size (30-80 nm) particles with a core composed mainly of TRIGLYCERIDES and a surface monolayer of PHOSPHOLIPIDS and CHOLESTEROL into which are imbedded the apolipoproteins B, E, and C. VLDL facilitates the transport of endogenously made triglycerides to extrahepatic tissues. As triglycerides and Apo C are removed, VLDL is converted to INTERMEDIATE-DENSITY LIPOPROTEINS, then to LOW-DENSITY LIPOPROTEINS from which cholesterol is delivered to the extrahepatic tissues.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
Esterases are hydrolase enzymes that catalyze the hydrolysis of ester bonds, converting esters into alcohols and acids, playing crucial roles in various biological processes including metabolism and detoxification.
A genus of zygomycetous fungi of the family Mucoraceae, order MUCORALES.
The severe infantile form of inherited lysosomal lipid storage diseases due to deficiency of acid lipase (STEROL ESTERASE). It is characterized by the accumulation of neutral lipids, particularly CHOLESTEROL ESTERS in leukocytes, fibroblasts, and hepatocytes. It is also known as Wolman's xanthomatosis and is an allelic variant of CHOLESTEROL ESTER STORAGE DISEASE.
A generic term for fats and lipoids, the alcohol-ether-soluble constituents of protoplasm, which are insoluble in water. They comprise the fats, fatty oils, essential oils, waxes, phospholipids, glycolipids, sulfolipids, aminolipids, chromolipids (lipochromes), and fatty acids. (Grant & Hackh's Chemical Dictionary, 5th ed)
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
A phospholipase that hydrolyzes the acyl group attached to the 1-position of PHOSPHOGLYCERIDES.
A condition of elevated levels of TRIGLYCERIDES in the blood.
Organic, monobasic acids derived from hydrocarbons by the equivalent of oxidation of a methyl group to an alcohol, aldehyde, and then acid. Fatty acids are saturated and unsaturated (FATTY ACIDS, UNSATURATED). (Grant & Hackh's Chemical Dictionary, 5th ed)
The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.
The rate dynamics in chemical or physical systems.
INFLAMMATION of the PANCREAS. Pancreatitis is classified as acute unless there are computed tomographic or endoscopic retrograde cholangiopancreatographic findings of CHRONIC PANCREATITIS (International Symposium on Acute Pancreatitis, Atlanta, 1992). The two most common forms of acute pancreatitis are ALCOHOLIC PANCREATITIS and gallstone pancreatitis.
The process of converting an acid into an alkyl or aryl derivative. Most frequently the process consists of the reaction of an acid with an alcohol in the presence of a trace of mineral acid as catalyst or the reaction of an acyl chloride with an alcohol. Esterification can also be accomplished by enzymatic processes.
Colloids formed by the combination of two immiscible liquids such as oil and water. Lipid-in-water emulsions are usually liquid, like milk or lotion. Water-in-lipid emulsions tend to be creams. The formation of emulsions may be aided by amphiphatic molecules that surround one component of the system to form MICELLES.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
A genus of yeast-like mitosporic Saccharomycetales fungi characterized by producing yeast cells, mycelia, pseudomycelia, and blastophores. It is commonly part of the normal flora of the skin, mouth, intestinal tract, and vagina, but can cause a variety of infections, including CANDIDIASIS; ONYCHOMYCOSIS; vulvovaginal candidiasis (CANDIDIASIS, VULVOVAGINAL), and thrush (see CANDIDIASIS, ORAL). (From Dorland, 28th ed)

Effective method for activity assay of lipase from Chromobacterium viscosum. (1/3030)

A method was devised for activity assay of the lipase [triacylglycerol acyl-hydrolase, EC 3.1.1.3] excreted from Chromobacterium viscosum into the culture medium; olive oil emulsified with the aid of Adekatol 45-S-8 (a non-ionic detergent, the ethoxylate of linear sec-alcohols having chain lengths of 10--16 carbon atoms) was used as the substrate. This method was specifically effective for Chromobacterium lipase acitvity assay, and was approximately twice as sensitive as the conventional method, in which polyvinyl alcohol is used for the emulsification of the substrate.  (+info)

Further studies on the mechanism of adrenaline-induced lipolysis in lipid micelles. (2/3030)

Lipase [EC 3.1.1.3] depleted lipid micelles, in which lipolysis was not elicited by adrenaline, were prepared from lipid micelles. When these lipase-depleted lipid micelles incubated with adipose tissue extract containing lipase activity, adrenaline-induced lipolysis was restored to almost the same level as that of native lipid micelles. Adrenaline-induced lipolysis was not restored when the lipase-depleted lipid micelles were homogenized or sonicated. Various tissue extracts from kidney, lung, liver, and pancreas, and post-heparin plasma, which contained lipase activity, restored adrenaline-induced lipolysis in lipase-depleted lipid micelles.  (+info)

Subcellullar localization, developmental expression and characterization of a liver triacylglycerol hydrolase. (3/3030)

The mechanism and enzymic activities responsible for the lipolysis of stored cytosolic triacylglycerol in liver and its re-esterification remain obscure. A candidate enzyme for lipolysis, a microsomal triacylglycerol hydrolase (TGH), was recently purified to homogeneity from pig liver and its kinetic properties were determined [Lehner and Verger (1997) Biochemistry 36, 1861-1868]. We have characterized the enzyme with regard to its species distribution, subcellular localization, developmental expression and reaction with lipase inhibitors. The hydrolase co-sediments with endoplasmic reticulum elements and is associated with isolated liver fat droplets. Immunocytochemical studies localize TGH exclusively to liver cells surrounding capillaries. Both TGH mRNA and protein are expressed in rats during weaning. The enzyme covalently binds tetrahydrolipstatin, an inhibitor of lipases and of triacylglycerol hydrolysis. The enzyme is absent from liver-derived cell lines (HepG2 and McArdle RH7777) known to be impaired in very-low-density lipoprotein (VLDL) assembly and secretion. The localization and developmental expression of TGH are consistent with a proposed role in triacylglycerol hydrolysis and with the proposal that some of the resynthesized triacylglycerol is utilized for VLDL secretion.  (+info)

Transgenic rabbits as models for atherosclerosis research. (4/3030)

Several characteristics of the rabbit make it an excellent model for the study of lipoprotein metabolism and atherosclerosis. New Zealand White (NZW) rabbits have low plasma total cholesterol concentrations, high cholesteryl ester transfer protein activity, low hepatic lipase (HL) activity, and lack an analogue of human apolipoprotein (apo) A-II, providing a unique system in which to assess the effects of human transgenes on plasma lipoproteins and atherosclerosis susceptibility. Additionally, rabbit models of human lipoprotein disorders, such as the Watanabe Heritable Hyperlipidemic (WHHL) and St. Thomas' Hospital strains, models of familial hypercholesterolemia and familial combined hyperlipidemia, respectively, allow for the assessment of candidate genes for potential use in the treatment of dyslipoproteinemic patients. To date, transgenes for human apo(a), apoA-I, apoB, apoE2, apoE3, HL, and lecithin:cholesterol acyltransferase (LCAT), as well as for rabbit apolipoprotein B mRNA-editing enzyme catalytic poly-peptide 1 (APOBEC-1), have been expressed in NZW rabbits, whereas only those for human apoA-I and LCAT have been introduced into the WHHL background. All of these transgenes have been shown to have significant effects on plasma lipoprotein concentrations. In both NZW and WHHL rabbits, human apoA-I expression was associated with a significant reduction in the extent of aortic atherosclerosis, which was similarly the case for LCAT in rabbits having at least one functional LDL receptor allele. Conversely, expression of apoE2 in NZW rabbits caused increased susceptibility to atherosclerosis. These studies provide new insights into the mechanisms responsible for the development of atherosclerosis, emphasizing the strength of the rabbit model in cardiovascular disease research.  (+info)

Elevated hepatic lipase activity and low levels of high density lipoprotein in a normotriglyceridemic, nonobese Turkish population. (5/3030)

Low levels of high density lipoprotein cholesterol (HDL-C) are associated with increased risk of coronary heart disease and, in the United States, are often associated with hypertriglyceridemia and obesity. In Turkey, low HDL-C levels are highly prevalent, 53% of men and 26% of women having HDL-C levels <35 mg/dl, in the absence of hypertriglyceridemia and obesity. In this study to investigate the cause of low HDL-C levels in Turks, various factors affecting HDL metabolism were assessed in normotriglyceridemic Turkish men and women living in Istanbul and in non-Turkish men and women living in San Francisco. Turkish men and women had significantly lower HDL-C levels than the San Francisco men and women, as well as markedly lower apolipoprotein A-I levels (25 and 39 mg/dl lower, respectively). In both Turkish and non-Turkish subjects, the mean body mass index was <27 kg/m2, the mean triglyceride level was <120 mg/dl, and the mean total cholesterol was 170-180 mg/dl. The mean hepatic triglyceride lipase activity was 21% and 31% higher in Turkish men and women, respectively, than in non-Turkish men and women, and remained higher even after subjects with a body mass index >50th percentile for men and women in the United States were excluded from the analysis. As no dietary or behavioral factors have been identified in the Turkish population that account for increased hepatic triglyceride lipase activity, the elevation most likely has a genetic basis. high density lipoprotein in a normotriglyceridemic, nonobese Turkish population.  (+info)

Characterization of functional residues in the interfacial recognition domain of lecithin cholesterol acyltransferase (LCAT). (6/3030)

Lecithin cholesterol acyltransferase (LCAT) is an interfacial enzyme active on both high-density (HDL) and low-density lipoproteins (LDL). Threading alignments of LCAT with lipases suggest that residues 50-74 form an interfacial recognition site and this hypothesis was tested by site-directed mutagenesis. The (delta56-68) deletion mutant had no activity on any substrate. Substitution of W61 with F, Y, L or G suggested that an aromatic residue is required for full enzymatic activity. The activity of the W61F and W61Y mutants was retained on HDL but decreased on LDL, possibly owing to impaired accessibility to the LDL lipid substrate. The decreased activity of the single R52A and K53A mutants on HDL and LDL and the severer effect of the double mutation suggested that these conserved residues contribute to the folding of the LCAT lid. The membrane-destabilizing properties of the LCAT 56-68 helical segment were demonstrated using the corresponding synthetic peptide. An M65N-N66M substitution decreased both the fusogenic properties of the peptide and the activity of the mutant enzyme on all substrates. These results suggest that the putative interfacial recognition domain of LCAT plays an important role in regulating the interaction of the enzyme with its organized lipoprotein substrates.  (+info)

Overexpression of human hepatic lipase and ApoE in transgenic rabbits attenuates response to dietary cholesterol and alters lipoprotein subclass distributions. (7/3030)

The effect of the expression of human hepatic lipase (HL) or human apoE on plasma lipoproteins in transgenic rabbits in response to dietary cholesterol was compared with the response of nontransgenic control rabbits. Supplementation of a chow diet with 0.3% cholesterol and 3.0% soybean oil for 10 weeks resulted in markedly increased levels of plasma cholesterol and VLDL and IDL in control rabbits as expected. Expression of either HL or apoE reduced plasma cholesterol response by 75% and 60%, respectively. The HL transgenic rabbits had substantial reductions in medium and small VLDL and IDL fractions but not in larger VLDL. LDL levels were also reduced, with a shift from larger, more buoyant to smaller, denser particles. In contrast, apoE transgenic rabbits had a marked reduction in the levels of large VLDLs, with a selective accumulation of IDLs and large buoyant LDLs. Combined expression of apoE and HL led to dramatic reductions of total cholesterol (85% versus controls) and of total VLDL+IDL+LDL (87% versus controls). HDL subclasses were remodeled by the expression of either transgene and accompanied by a decrease in HDL cholesterol compared with controls. HL expression reduced all subclasses except for HDL2b and HDL2a, and expression of apoE reduced large HDL1 and HDL2b. Extreme HDL reductions (92% versus controls) were observed in the combined HL+apoE transgenic rabbits. These results demonstrate that human HL and apoE have complementary and synergistic functions in plasma cholesterol and lipoprotein metabolism.  (+info)

Identification of the tliDEF ABC transporter specific for lipase in Pseudomonas fluorescens SIK W1. (8/3030)

Pseudomonas fluorescens, a gram-negative psychrotrophic bacterium, secretes a thermostable lipase into the extracellular medium. In our previous study, the lipase of P. fluorescens SIK W1 was cloned and expressed in Escherichia coli, but it accumulated as inactive inclusion bodies. Amino acid sequence analysis of the lipase revealed a potential C-terminal targeting sequence recognized by the ATP-binding cassette (ABC) transporter. The genetic loci around the lipase gene were searched, and a secretory gene was identified. Nucleotide sequencing of an 8.5-kb DNA fragment revealed three components of the ABC transporter, tliD, tliE, and tliF, upstream of the lipase gene, tliA. In addition, genes encoding a protease and a protease inhibitor were located upstream of tliDEF. tliDEF showed high similarity to ABC transporters of Pseudomonas aeruginosa alkaline protease, Erwinia chrysanthemi protease, Serratia marcescens lipase, and Pseudomonas fluorescens CY091 protease. tliDEF and the lipase structural gene in a single operon were sufficient for E. coli cells to secrete the lipase. In addition, E. coli harboring the lipase gene secreted the lipase by complementation of tliDEF in a different plasmid. The ABC transporter of P. fluorescens was optimally functional at 20 and 25 degrees C, while the ABC transporter, aprD, aprE, and aprF, of P. aeruginosa secreted the lipase irrespective of temperature between 20 and 37 degrees C. These results demonstrated that the lipase is secreted by the P. fluorescens SIK W1 ABC transporter, which is organized as an operon with tliA, and that its secretory function is temperature dependent.  (+info)

Lipase is an enzyme that is produced by the pancreas and found in the digestive system of most organisms. Its primary function is to catalyze the hydrolysis of fats (triglycerides) into smaller molecules, such as fatty acids and glycerol, which can then be absorbed by the intestines and utilized for energy or stored for later use.

In medical terms, lipase levels in the blood are often measured to diagnose or monitor conditions that affect the pancreas, such as pancreatitis (inflammation of the pancreas), pancreatic cancer, or cystic fibrosis. Elevated lipase levels may indicate damage to the pancreas and its ability to produce digestive enzymes.

Lipoprotein lipase (LPL) is an enzyme that plays a crucial role in the metabolism of lipids. It is responsible for breaking down triglycerides, which are the main constituent of dietary fats and chylomicrons, into fatty acids and glycerol. These products are then taken up by cells for energy production or storage.

LPL is synthesized in various tissues, including muscle and fat, where it is attached to the inner lining of blood vessels (endothelium). The enzyme is activated when it comes into contact with lipoprotein particles, such as chylomicrons and very-low-density lipoproteins (VLDL), which transport triglycerides in the bloodstream.

Deficiencies or mutations in LPL can lead to various metabolic disorders, including hypertriglyceridemia, a condition characterized by high levels of triglycerides in the blood. Conversely, overexpression of LPL has been associated with increased risk of atherosclerosis due to excessive uptake of fatty acids by macrophages and their conversion into foam cells, which contribute to plaque formation in the arteries.

Monoacylglycerol lipases (MAGLs) are a type of enzyme that play a role in the metabolism of lipids, specifically by breaking down monoacylglycerols into glycerol and free fatty acids. Monoacylglycerols are formed during the digestion of dietary fats and are also produced endogenously as a result of the breakdown of complex lipids.

MAGLs are widely distributed throughout the body, but are particularly abundant in tissues that utilize large amounts of fatty acids for energy, such as the liver, heart, and skeletal muscle. In addition to their role in lipid metabolism, MAGLs have been implicated in various physiological processes, including inflammation, pain perception, and cancer.

Inhibition of MAGL activity has been proposed as a potential therapeutic strategy for the treatment of various diseases, including obesity, diabetes, and neurodegenerative disorders. However, further research is needed to fully understand the role of MAGLs in these processes and to determine the safety and efficacy of MAGL inhibitors as drugs.

A sterol esterase is an enzyme that catalyzes the hydrolysis of sterol esters, which are fatty acid esters of sterols (such as cholesterol) that are commonly found in lipoproteins and cell membranes. Sterol esterases play a crucial role in the metabolism of lipids by breaking down sterol esters into free sterols and free fatty acids, which can then be used in various biochemical processes.

There are several types of sterol esterases that have been identified, including:

1. Cholesteryl esterase (CE): This enzyme is responsible for hydrolyzing cholesteryl esters in the intestine and liver. It plays a critical role in the absorption and metabolism of dietary cholesterol.
2. Hormone-sensitive lipase (HSL): This enzyme is involved in the hydrolysis of sterol esters in adipose tissue, as well as other lipids such as triacylglycerols. It is regulated by hormones such as insulin and catecholamines.
3. Carboxylesterase (CES): This enzyme is a broad-specificity esterase that can hydrolyze various types of esters, including sterol esters. It is found in many tissues throughout the body.

Sterol esterases are important targets for drug development, as inhibiting these enzymes can have therapeutic effects in a variety of diseases, such as obesity, diabetes, and cardiovascular disease.

Colipases are small protein enzymes that activate and work together with pancreatic lipases to digest dietary fats in the small intestine. They are produced by the pancreas and secreted into the duodenum as part of the pancreatic juice. Colipases help to stabilize and orient the lipase enzyme on the surface of fat droplets, allowing it to efficiently hydrolyze triacylglycerols into monoacylglycerols, free fatty acids, and glycerol. This process is crucial for the absorption of dietary fats in the human body.

Lipolysis is the process by which fat cells (adipocytes) break down stored triglycerides into glycerol and free fatty acids. This process occurs when the body needs to use stored fat as a source of energy, such as during fasting, exercise, or in response to certain hormonal signals. The breakdown products of lipolysis can be used directly by cells for energy production or can be released into the bloodstream and transported to other tissues for use. Lipolysis is regulated by several hormones, including adrenaline (epinephrine), noradrenaline (norepinephrine), cortisol, glucagon, and growth hormone, which act on lipases, enzymes that mediate the breakdown of triglycerides.

Triolein is a type of triglyceride, which is a kind of fat molecule. More specifically, triolein is the triglyceride formed from three molecules of oleic acid, a common monounsaturated fatty acid. It is often used in scientific research and studies involving lipid metabolism, and it can be found in various vegetable oils and animal fats.

Triglycerides are the most common type of fat in the body, and they're found in the food we eat. They're carried in the bloodstream to provide energy to the cells in our body. High levels of triglycerides in the blood can increase the risk of heart disease, especially in combination with other risk factors such as high LDL (bad) cholesterol, low HDL (good) cholesterol, and high blood pressure.

It's important to note that while triglycerides are a type of fat, they should not be confused with cholesterol, which is a waxy substance found in the cells of our body. Both triglycerides and cholesterol are important for maintaining good health, but high levels of either can increase the risk of heart disease.

Triglyceride levels are measured through a blood test called a lipid panel or lipid profile. A normal triglyceride level is less than 150 mg/dL. Borderline-high levels range from 150 to 199 mg/dL, high levels range from 200 to 499 mg/dL, and very high levels are 500 mg/dL or higher.

Elevated triglycerides can be caused by various factors such as obesity, physical inactivity, excessive alcohol consumption, smoking, and certain medical conditions like diabetes, hypothyroidism, and kidney disease. Medications such as beta-blockers, steroids, and diuretics can also raise triglyceride levels.

Lifestyle changes such as losing weight, exercising regularly, eating a healthy diet low in saturated and trans fats, avoiding excessive alcohol consumption, and quitting smoking can help lower triglyceride levels. In some cases, medication may be necessary to reduce triglycerides to recommended levels.

Rhizopus is a genus of saprophytic fungi that belong to the family Mucoraceae. These fungi are commonly found in soil, decaying vegetation, and fruits. They are characterized by the presence of rhizoids, which are multicellular filaments that anchor the fungus to its substrate.

Rhizopus species are known to produce spores in large numbers, which can be dispersed through the air and cause infections in humans, particularly in individuals with weakened immune systems. One of the most common diseases caused by Rhizopus is mucormycosis, a serious and often life-threatening fungal infection that can affect various organs, including the sinuses, lungs, brain, and skin.

It's worth noting that while Rhizopus species are important pathogens in certain populations, they also have beneficial uses. For example, some species of Rhizopus are used in the production of tempeh, a traditional Indonesian food made from fermented soybeans.

Geotrichum is a genus of saprophytic fungi that can be found in various environments, including soil, water, and organic matter. The most common species is Geotrichum candidum, which is often associated with dairy products and is used in the production of certain cheeses. However, G. candidum and other Geotrichum species can also be isolated from human respiratory samples and are occasionally identified as causes of respiratory tract infections or allergic reactions in immunocompromised individuals.

In a medical context, Geotrichum infection is called geotrichosis. It primarily affects the lungs and may present with symptoms such as cough, fever, chest pain, and shortness of breath. In severe cases, the infection can spread to other organs, including the brain, causing meningitis or brain abscesses. Geotrichum infections are typically treated with antifungal medications, such as amphotericin B, fluconazole, or itraconazole.

It is important to note that Geotrichum species are commonly found in the environment and on human skin without causing any harm. Invasive geotrichosis is relatively rare and primarily affects individuals with weakened immune systems due to conditions like HIV/AIDS, cancer, or organ transplantation.

Hyperlipoproteinemia Type I, also known as Familial Lipoprotein Lipase Deficiency, is a rare genetic disorder characterized by an absence or deficiency of the enzyme lipoprotein lipase. This enzyme is responsible for breaking down chylomicrons, which are large lipoprotein particles that transport dietary triglycerides from the intestines to the liver and peripheral tissues.

As a result of this deficiency, chylomicrons accumulate in the bloodstream, leading to elevated levels of triglycerides (hypertriglyceridemia) and chylomicrons (chylomiconemia). This condition can cause eruptive xanthomas, which are collections of lipid-laden foam cells that form under the skin, and recurrent pancreatitis, which is inflammation of the pancreas.

Hyperlipoproteinemia Type I is inherited in an autosomal recessive manner, meaning that an individual must inherit two copies of the mutated gene, one from each parent, to develop the condition. Treatment typically involves a low-fat diet and medications to reduce triglyceride levels.

The pancreas is a glandular organ located in the abdomen, posterior to the stomach. It has both exocrine and endocrine functions. The exocrine portion of the pancreas consists of acinar cells that produce and secrete digestive enzymes into the duodenum via the pancreatic duct. These enzymes help in the breakdown of proteins, carbohydrates, and fats in food.

The endocrine portion of the pancreas consists of clusters of cells called islets of Langerhans, which include alpha, beta, delta, and F cells. These cells produce and secrete hormones directly into the bloodstream, including insulin, glucagon, somatostatin, and pancreatic polypeptide. Insulin and glucagon are critical regulators of blood sugar levels, with insulin promoting glucose uptake and storage in tissues and glucagon stimulating glycogenolysis and gluconeogenesis to raise blood glucose when it is low.

Carboxylic ester hydrolases are a class of enzymes that catalyze the hydrolysis of ester bonds in carboxylic acid esters, producing alcohols and carboxylates. This group includes several subclasses of enzymes such as esterases, lipases, and thioesterases. These enzymes play important roles in various biological processes, including metabolism, detoxification, and signal transduction. They are widely used in industrial applications, such as the production of biodiesel, pharmaceuticals, and food ingredients.

Apolipoprotein C-II (ApoC-II) is a type of apolipoprotein, which are proteins that bind to lipids to form lipoprotein complexes. ApoC-II is a component of several lipoproteins, including very low-density lipoproteins (VLDL) and chylomicrons, which are responsible for the transport of fat molecules, such as triglycerides and cholesterol, in the bloodstream.

ApoC-II plays a crucial role in the activation of lipoprotein lipase, an enzyme that breaks down triglycerides in VLDL and chylomicrons into fatty acids, which can then be taken up by cells for energy production or storage. Therefore, ApoC-II deficiency can lead to hypertriglyceridemia, a condition characterized by high levels of triglycerides in the blood.

In addition to its role in lipid metabolism, ApoC-II has been implicated in the development and progression of atherosclerosis, a chronic inflammatory disease that affects the arteries and can lead to serious cardiovascular complications, such as heart attack and stroke.

Heparin is defined as a highly sulfated glycosaminoglycan (a type of polysaccharide) that is widely present in many tissues, but is most commonly derived from the mucosal tissues of mammalian lungs or intestinal mucosa. It is an anticoagulant that acts as an inhibitor of several enzymes involved in the blood coagulation cascade, primarily by activating antithrombin III which then neutralizes thrombin and other clotting factors.

Heparin is used medically to prevent and treat thromboembolic disorders such as deep vein thrombosis, pulmonary embolism, and certain types of heart attacks. It can also be used during hemodialysis, cardiac bypass surgery, and other medical procedures to prevent the formation of blood clots.

It's important to note that while heparin is a powerful anticoagulant, it does not have any fibrinolytic activity, meaning it cannot dissolve existing blood clots. Instead, it prevents new clots from forming and stops existing clots from growing larger.

Glycerides are esters formed from glycerol and one, two, or three fatty acids. They include monoglycerides (one fatty acid), diglycerides (two fatty acids), and triglycerides (three fatty acids). Triglycerides are the main constituents of natural fats and oils, and they are a major form of energy storage in animals and plants. High levels of triglycerides in the blood, also known as hypertriglyceridemia, can increase the risk of heart disease and stroke.

Chylomicrons are a type of lipoprotein that are responsible for carrying dietary lipids, such as triglycerides and cholesterol, from the intestines to other parts of the body through the lymphatic system and bloodstream. They are the largest lipoproteins and are composed of an outer layer of phospholipids, free cholesterol, and apolipoproteins, which surrounds a core of triglycerides and cholesteryl esters. Chylomicrons are produced in the intestinal mucosa after a meal containing fat, and their production is stimulated by the hormone cholecystokinin. Once in the bloodstream, chylomicrons interact with other lipoproteins and enzymes to deliver their lipid cargo to various tissues, including muscle and adipose tissue, where they are used for energy or stored for later use.

Adipose tissue, also known as fatty tissue, is a type of connective tissue that is composed mainly of adipocytes (fat cells). It is found throughout the body, but is particularly abundant in the abdominal cavity, beneath the skin, and around organs such as the heart and kidneys.

Adipose tissue serves several important functions in the body. One of its primary roles is to store energy in the form of fat, which can be mobilized and used as an energy source during periods of fasting or exercise. Adipose tissue also provides insulation and cushioning for the body, and produces hormones that help regulate metabolism, appetite, and reproductive function.

There are two main types of adipose tissue: white adipose tissue (WAT) and brown adipose tissue (BAT). WAT is the more common form and is responsible for storing energy as fat. BAT, on the other hand, contains a higher number of mitochondria and is involved in heat production and energy expenditure.

Excessive accumulation of adipose tissue can lead to obesity, which is associated with an increased risk of various health problems such as diabetes, heart disease, and certain types of cancer.

Hydrolysis is a chemical process, not a medical one. However, it is relevant to medicine and biology.

Hydrolysis is the breakdown of a chemical compound due to its reaction with water, often resulting in the formation of two or more simpler compounds. In the context of physiology and medicine, hydrolysis is a crucial process in various biological reactions, such as the digestion of food molecules like proteins, carbohydrates, and fats. Enzymes called hydrolases catalyze these hydrolysis reactions to speed up the breakdown process in the body.

Immobilized enzymes refer to enzymes that have been restricted or fixed in a specific location and are unable to move freely. This is typically achieved through physical or chemical methods that attach the enzyme to a solid support or matrix. The immobilization of enzymes can provide several advantages, including increased stability, reusability, and ease of separation from the reaction mixture.

Immobilized enzymes are widely used in various industrial applications, such as biotransformations, biosensors, and diagnostic kits. They can also be used for the production of pharmaceuticals, food additives, and other fine chemicals. The immobilization techniques include adsorption, covalent binding, entrapment, and cross-linking.

Adsorption involves physically attaching the enzyme to a solid support through weak forces such as van der Waals interactions or hydrogen bonding. Covalent binding involves forming chemical bonds between the enzyme and the support matrix. Entrapment involves encapsulating the enzyme within a porous matrix, while cross-linking involves chemically linking multiple enzyme molecules together to form a stable structure.

Overall, immobilized enzymes offer several advantages over free enzymes, including improved stability, reusability, and ease of separation from the reaction mixture, making them valuable tools in various industrial applications.

Carboxylesterase is a type of enzyme that catalyzes the hydrolysis of ester bonds in carboxylic acid esters, producing alcohol and carboxylate products. These enzymes are widely distributed in various tissues, including the liver, intestines, and plasma. They play important roles in detoxification, metabolism, and the breakdown of xenobiotics (foreign substances) in the body.

Carboxylesterases can also catalyze the reverse reaction, forming esters from alcohols and carboxylates, which is known as transesterification or esterification. This activity has applications in industrial processes and biotechnology.

There are several families of carboxylesterases, with different substrate specificities, kinetic properties, and tissue distributions. These enzymes have been studied for their potential use in therapeutics, diagnostics, and drug delivery systems.

The liver is a large, solid organ located in the upper right portion of the abdomen, beneath the diaphragm and above the stomach. It plays a vital role in several bodily functions, including:

1. Metabolism: The liver helps to metabolize carbohydrates, fats, and proteins from the food we eat into energy and nutrients that our bodies can use.
2. Detoxification: The liver detoxifies harmful substances in the body by breaking them down into less toxic forms or excreting them through bile.
3. Synthesis: The liver synthesizes important proteins, such as albumin and clotting factors, that are necessary for proper bodily function.
4. Storage: The liver stores glucose, vitamins, and minerals that can be released when the body needs them.
5. Bile production: The liver produces bile, a digestive juice that helps to break down fats in the small intestine.
6. Immune function: The liver plays a role in the immune system by filtering out bacteria and other harmful substances from the blood.

Overall, the liver is an essential organ that plays a critical role in maintaining overall health and well-being.

Amylases are enzymes that break down complex carbohydrates, such as starch and glycogen, into simpler sugars like maltose, glucose, and maltotriose. There are several types of amylases found in various organisms, including humans.

In humans, amylases are produced by the pancreas and salivary glands. Pancreatic amylase is released into the small intestine where it helps to digest dietary carbohydrates. Salivary amylase, also known as alpha-amylase, is secreted into the mouth and begins breaking down starches in food during chewing.

Deficiency or absence of amylases can lead to difficulties in digesting carbohydrates and may cause symptoms such as bloating, diarrhea, and abdominal pain. Elevated levels of amylase in the blood may indicate conditions such as pancreatitis, pancreatic cancer, or other disorders affecting the pancreas.

Lipid metabolism is the process by which the body breaks down and utilizes lipids (fats) for various functions, such as energy production, cell membrane formation, and hormone synthesis. This complex process involves several enzymes and pathways that regulate the digestion, absorption, transport, storage, and consumption of fats in the body.

The main types of lipids involved in metabolism include triglycerides, cholesterol, phospholipids, and fatty acids. The breakdown of these lipids begins in the digestive system, where enzymes called lipases break down dietary fats into smaller molecules called fatty acids and glycerol. These molecules are then absorbed into the bloodstream and transported to the liver, which is the main site of lipid metabolism.

In the liver, fatty acids may be further broken down for energy production or used to synthesize new lipids. Excess fatty acids may be stored as triglycerides in specialized cells called adipocytes (fat cells) for later use. Cholesterol is also metabolized in the liver, where it may be used to synthesize bile acids, steroid hormones, and other important molecules.

Disorders of lipid metabolism can lead to a range of health problems, including obesity, diabetes, cardiovascular disease, and non-alcoholic fatty liver disease (NAFLD). These conditions may be caused by genetic factors, lifestyle habits, or a combination of both. Proper diagnosis and management of lipid metabolism disorders typically involves a combination of dietary changes, exercise, and medication.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Apolipoprotein C (apoC) is a group of proteins that are associated with lipoproteins, which are complex particles composed of lipids and proteins that play a crucial role in the transport and metabolism of lipids in the body. There are three main types of apoC proteins: apoC-I, apoC-II, and apoC-III.

ApoC-I is involved in the regulation of lipoprotein metabolism and has been shown to inhibit the activity of cholesteryl ester transfer protein (CETP), which is an enzyme that facilitates the transfer of cholesteryl esters from high-density lipoproteins (HDL) to low-density lipoproteins (LDL) and very low-density lipoproteins (VLDL).

ApoC-II is a cofactor for lipoprotein lipase, an enzyme that hydrolyzes triglycerides in chylomicrons and VLDL, leading to the formation of smaller, denser lipoproteins. A deficiency in apoC-II can lead to hypertriglyceridemia, a condition characterized by elevated levels of triglycerides in the blood.

ApoC-III is also involved in the regulation of lipoprotein metabolism and has been shown to inhibit the activity of lipoprotein lipase and CETP. Elevated levels of apoC-III have been associated with an increased risk of cardiovascular disease, possibly due to its effects on lipoprotein metabolism.

In summary, apolipoprotein C is a group of proteins that are involved in the regulation of lipoprotein metabolism and have important roles in the transport and metabolism of lipids in the body.

Lipoproteins are complex particles composed of multiple proteins and lipids (fats) that play a crucial role in the transport and metabolism of fat molecules in the body. They consist of an outer shell of phospholipids, free cholesterols, and apolipoproteins, enclosing a core of triglycerides and cholesteryl esters.

There are several types of lipoproteins, including:

1. Chylomicrons: These are the largest lipoproteins and are responsible for transporting dietary lipids from the intestines to other parts of the body.
2. Very-low-density lipoproteins (VLDL): Produced by the liver, VLDL particles carry triglycerides to peripheral tissues for energy storage or use.
3. Low-density lipoproteins (LDL): Often referred to as "bad cholesterol," LDL particles transport cholesterol from the liver to cells throughout the body. High levels of LDL in the blood can lead to plaque buildup in artery walls and increase the risk of heart disease.
4. High-density lipoproteins (HDL): Known as "good cholesterol," HDL particles help remove excess cholesterol from cells and transport it back to the liver for excretion or recycling. Higher levels of HDL are associated with a lower risk of heart disease.

Understanding lipoproteins and their roles in the body is essential for assessing cardiovascular health and managing risks related to heart disease and stroke.

VLDL (Very Low-Density Lipoproteins) are a type of lipoprotein that play a crucial role in the transport and metabolism of fat molecules, known as triglycerides, in the body. They are produced by the liver and consist of a core of triglycerides surrounded by a shell of proteins called apolipoproteins, phospholipids, and cholesterol.

VLDL particles are responsible for delivering fat molecules from the liver to peripheral tissues throughout the body, where they can be used as an energy source or stored for later use. During this process, VLDL particles lose triglycerides and acquire more cholesterol, transforming into intermediate-density lipoproteins (IDL) and eventually low-density lipoproteins (LDL), which are also known as "bad" cholesterol.

Elevated levels of VLDL in the blood can contribute to the development of cardiovascular disease due to their association with increased levels of triglycerides and LDL cholesterol, as well as decreased levels of high-density lipoproteins (HDL), which are considered "good" cholesterol.

Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).

Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.

Substrate specificity can be categorized as:

1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.

Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.

Esterases are a group of enzymes that catalyze the hydrolysis of ester bonds in esters, producing alcohols and carboxylic acids. They are widely distributed in plants, animals, and microorganisms and play important roles in various biological processes, such as metabolism, digestion, and detoxification.

Esterases can be classified into several types based on their substrate specificity, including carboxylesterases, cholinesterases, lipases, and phosphatases. These enzymes have different structures and mechanisms of action but all share the ability to hydrolyze esters.

Carboxylesterases are the most abundant and diverse group of esterases, with a wide range of substrate specificity. They play important roles in the metabolism of drugs, xenobiotics, and lipids. Cholinesterases, on the other hand, specifically hydrolyze choline esters, such as acetylcholine, which is an important neurotransmitter in the nervous system. Lipases are a type of esterase that preferentially hydrolyzes triglycerides and plays a crucial role in fat digestion and metabolism. Phosphatases are enzymes that remove phosphate groups from various molecules, including esters, and have important functions in signal transduction and other cellular processes.

Esterases can also be used in industrial applications, such as in the production of biodiesel, detergents, and food additives. They are often produced by microbial fermentation or extracted from plants and animals. The use of esterases in biotechnology is an active area of research, with potential applications in biofuel production, bioremediation, and medical diagnostics.

Rhizomucor is a genus of fungi in the family Mucoraceae. It includes several species that are commonly found in soil, decaying organic matter, and air. Some species of Rhizomucor can cause mucormycosis, a serious and potentially life-threatening invasive fungal infection that primarily affects people with weakened immune systems.

Mucormycosis caused by Rhizomucor species often involves the sinuses, brain, and lungs, and can also spread to other parts of the body through the bloodstream. Symptoms may include fever, cough, shortness of breath, headache, nasal congestion, and black lesions on the skin. Treatment typically involves a combination of antifungal medications, surgical debridement, and management of underlying medical conditions that increase the risk of infection.

It's worth noting that mucormycosis is a rare but serious infection, and prompt diagnosis and treatment are essential for improving outcomes. Preventive measures such as avoiding contact with contaminated soil or water, wearing protective masks in dusty environments, and maintaining good hygiene can help reduce the risk of infection.

Wolman disease is a rare inherited disorder of lipid metabolism, specifically affecting the enzyme acid lipase that is responsible for breaking down cholesteryl esters and triglycerides in lysosomes. This autosomal recessive condition leads to an accumulation of these fatty substances in various tissues and organs, including the liver, spleen, intestines, adrenal glands, and lymph nodes.

The symptoms of Wolman disease typically appear within the first few months of life and can include vomiting, diarrhea, failure to thrive, abdominal distention, and severe malnutrition. Other features may consist of hepatosplenomegaly (enlarged liver and spleen), calcification of adrenal glands, and progressive deterioration of the nervous system. The disease often results in death within the first two years of life if left untreated.

A related condition called acid lipase deficiency or Cholesteryl Ester Storage Disease (CESD) has a later onset and milder symptoms compared to Wolman disease, as it affects only one form of acid lipase enzyme.

Lipids are a broad group of organic compounds that are insoluble in water but soluble in nonpolar organic solvents. They include fats, waxes, sterols, fat-soluble vitamins (such as vitamins A, D, E, and K), monoglycerides, diglycerides, triglycerides, and phospholipids. Lipids serve many important functions in the body, including energy storage, acting as structural components of cell membranes, and serving as signaling molecules. High levels of certain lipids, particularly cholesterol and triglycerides, in the blood are associated with an increased risk of cardiovascular disease.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Phospholipase A1 (PLA1) is an enzyme that catalyzes the hydrolysis of the ester bond at the sn-1 position of glycerophospholipids, resulting in the production of free fatty acids and lysophospholipids. This enzyme plays a crucial role in various biological processes, including cell signaling, membrane remodeling, and inflammation. PLA1 is widely distributed in nature and can be found in different organisms, such as bacteria, plants, and animals. In humans, PLA1 is involved in several physiological and pathological conditions, including lipid metabolism, atherosclerosis, neurodegenerative diseases, and cancer.

Hypertriglyceridemia is a medical condition characterized by an elevated level of triglycerides in the blood. Triglycerides are a type of fat (lipid) found in your blood that can increase the risk of developing heart disease, especially when levels are very high.

In general, hypertriglyceridemia is defined as having triglyceride levels greater than 150 milligrams per deciliter (mg/dL) of blood. However, the specific definition of hypertriglyceridemia may vary depending on individual risk factors and medical history.

Hypertriglyceridemia can be caused by a variety of factors, including genetics, obesity, physical inactivity, excessive alcohol consumption, and certain medications. In some cases, it may also be a secondary consequence of other medical conditions such as diabetes or hypothyroidism. Treatment for hypertriglyceridemia typically involves lifestyle modifications such as dietary changes, increased exercise, and weight loss, as well as medication if necessary.

Fatty acids are carboxylic acids with a long aliphatic chain, which are important components of lipids and are widely distributed in living organisms. They can be classified based on the length of their carbon chain, saturation level (presence or absence of double bonds), and other structural features.

The two main types of fatty acids are:

1. Saturated fatty acids: These have no double bonds in their carbon chain and are typically solid at room temperature. Examples include palmitic acid (C16:0) and stearic acid (C18:0).
2. Unsaturated fatty acids: These contain one or more double bonds in their carbon chain and can be further classified into monounsaturated (one double bond) and polyunsaturated (two or more double bonds) fatty acids. Examples of unsaturated fatty acids include oleic acid (C18:1, monounsaturated), linoleic acid (C18:2, polyunsaturated), and alpha-linolenic acid (C18:3, polyunsaturated).

Fatty acids play crucial roles in various biological processes, such as energy storage, membrane structure, and cell signaling. Some essential fatty acids cannot be synthesized by the human body and must be obtained through dietary sources.

Enzyme stability refers to the ability of an enzyme to maintain its structure and function under various environmental conditions, such as temperature, pH, and the presence of denaturants or inhibitors. A stable enzyme retains its activity and conformation over time and across a range of conditions, making it more suitable for industrial and therapeutic applications.

Enzymes can be stabilized through various methods, including chemical modification, immobilization, and protein engineering. Understanding the factors that affect enzyme stability is crucial for optimizing their use in biotechnology, medicine, and research.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

Pancreatitis is a medical condition characterized by inflammation of the pancreas, a gland located in the abdomen that plays a crucial role in digestion and regulating blood sugar levels. The inflammation can be acute (sudden and severe) or chronic (persistent and recurring), and it can lead to various complications if left untreated.

Acute pancreatitis often results from gallstones or excessive alcohol consumption, while chronic pancreatitis may be caused by long-term alcohol abuse, genetic factors, autoimmune conditions, or metabolic disorders like high triglyceride levels. Symptoms of acute pancreatitis include severe abdominal pain, nausea, vomiting, fever, and increased heart rate, while chronic pancreatitis may present with ongoing abdominal pain, weight loss, diarrhea, and malabsorption issues due to impaired digestive enzyme production. Treatment typically involves supportive care, such as intravenous fluids, pain management, and addressing the underlying cause. In severe cases, hospitalization and surgery may be necessary.

Esterification is a chemical reaction that involves the conversion of an alcohol and a carboxylic acid into an ester, typically through the removal of a molecule of water. This reaction is often catalyzed by an acid or a base, and it is a key process in organic chemistry. Esters are commonly found in nature and are responsible for the fragrances of many fruits and flowers. They are also important in the production of various industrial and consumer products, including plastics, resins, and perfumes.

An emulsion is a type of stable mixture of two immiscible liquids, such as oil and water, which are normally unable to mix together uniformly. In an emulsion, one liquid (the dispersed phase) is broken down into small droplets and distributed throughout the other liquid (the continuous phase), creating a stable, cloudy mixture.

In medical terms, emulsions can be used in various pharmaceutical and cosmetic applications. For example, certain medications may be formulated as oil-in-water or water-in-oil emulsions to improve their absorption, stability, or palatability. Similarly, some skincare products and makeup removers contain emulsifiers that help create stable mixtures of water and oils, allowing for effective cleansing and moisturizing.

Emulsions can also occur naturally in the body, such as in the digestion of fats. The bile salts produced by the liver help to form small droplets of dietary lipids (oil) within the watery environment of the small intestine, allowing for efficient absorption and metabolism of these nutrients.

Hydrogen-ion concentration, also known as pH, is a measure of the acidity or basicity of a solution. It is defined as the negative logarithm (to the base 10) of the hydrogen ion activity in a solution. The standard unit of measurement is the pH unit. A pH of 7 is neutral, less than 7 is acidic, and greater than 7 is basic.

In medical terms, hydrogen-ion concentration is important for maintaining homeostasis within the body. For example, in the stomach, a high hydrogen-ion concentration (low pH) is necessary for the digestion of food. However, in other parts of the body such as blood, a high hydrogen-ion concentration can be harmful and lead to acidosis. Conversely, a low hydrogen-ion concentration (high pH) in the blood can lead to alkalosis. Both acidosis and alkalosis can have serious consequences on various organ systems if not corrected.

'Candida' is a type of fungus (a form of yeast) that is commonly found on the skin and inside the body, including in the mouth, throat, gut, and vagina, in small amounts. It is a part of the normal microbiota and usually does not cause any problems. However, an overgrowth of Candida can lead to infections known as candidiasis or thrush. Common sites for these infections include the skin, mouth, throat, and genital areas. Some factors that can contribute to Candida overgrowth are a weakened immune system, certain medications (such as antibiotics and corticosteroids), diabetes, pregnancy, poor oral hygiene, and wearing damp or tight-fitting clothing. Common symptoms of candidiasis include itching, redness, pain, and discharge. Treatment typically involves antifungal medication, either topical or oral, depending on the site and severity of the infection.

... (/ˈlaɪpeɪs, ˈlaɪpeɪz/ LY-payss, LY-payz) is a family of enzymes that catalyzes the hydrolysis of fats. Some lipases ... Other lipases include LIPH, LIPI, LIPJ, LIPK, LIPM, LIPN, MGLL, DAGLA, DAGLB, and CEL. In the commercial sphere, lipases are ... Lipases are generally animal sourced, but can also be sourced microbially[citation needed]. Blood tests for lipase may be used ... Measured serum lipase values may vary depending on the method of analysis.[citation needed] Lipase assist in the breakdown of ...
It has a pH optimum of 3-6. Gastric lipase, together with lingual lipase, comprise the two acidic lipases. These lipases, ... This leaves the acidic lipases less efficient than alkaline lipases. Gastric lipase is a polypeptide of 371 residues in length ... with gastric lipase contributing the most of the two acidic lipases. In neonates, acidic lipases are much more important, ... Gastric lipase, also known as LIPF, is an enzymatic protein that, in humans, is encoded by the LIPF gene. Gastric lipase is an ...
... triglyceride lipase, liver lipase, hepatic monoacylglycerol acyltransferase). Pancreatic lipase Gastric lipase Lingual lipase ... meito Sangyo OF lipase, hepatic lipase, lipazin, post-heparin plasma protamine-resistant lipase, salt-resistant post-heparin ... This family was also called class 3 lipases as they are only distantly related to other lipase families. DAGLA; DAGLB; ... The enzyme triacylglycerol lipase (also triglyceride lipase, EC 3.1.1.3;systematic name triacylglycerol acylhydrolase) ...
... are substances used to reduce the activity of lipases found in the intestine. Lipases are secreted by the ... Lipase inhibitors covalently bond to the active serine site on lipases. This covalent bond is strong, meaning the lipase ... Likewise, lipase inhibitors are not absorbed into the bloodstream. Lipase inhibitors bind to lipase enzymes in the intestine, ... Lipase inhibitors can be found naturally in plants and can also be produced as pharmaceutical drugs. Some lipase inhibitors ...
... is a member of the lipase gene family, which includes pancreatic lipase, hepatic lipase, and endothelial lipase. It is a water- ... "Entrez Gene: LPL lipoprotein lipase". Wang H, Eckel RH (2009). "Lipoprotein lipase: from gene to obesity". Am J Physiol ... GeneReviews/NCBI/NIH/UW entry on Familial Lipoprotein Lipase Deficiency Gene therapy for lipoprotein lipase deficiency ... Lipoprotein lipase has been shown to interact with LRP1. It is also a ligand for α2M, GP330, and VLDL receptors. LPL has been ...
... , also known as DAG lipase, DAGL, or DGL, is an enzyme that catalyzes the hydrolysis of diacylglycerol, ... Diacylglycerol lipase uses a Serine-Aspartate-Histidine catalytic triad to hydrolyze the ester bond of an acyl chain from ... Diacylglycerol lipase has been identified as a tunable target in the endocannabinoid system. It has been the subject of ... Diacylglycerol+Lipase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) EC 3.1.1.116 Portal: Biology ( ...
... (HL), also called hepatic triglyceride lipase (HTGL) or LIPC (for "lipase, hepatic"), is a form of lipase, ... Hepatic lipase is coded by chromosome 15 and its gene is also often referred to as HTGL or LIPC. Hepatic lipase is expressed ... Hegele RA, Little JA, Connelly PW (August 1991). "Compound heterozygosity for mutant hepatic lipase in familial hepatic lipase ... mapping of loci for lipoprotein lipase to 8p22 and hepatic lipase to 15q21". Genomics. 1 (2): 138-44. doi:10.1016/0888-7543(87) ...
... (EC 3.1.1.23; systematic name glycerol-ester acylhydrolase, also known as MAG lipase, acylglycerol ... Monoacylglycerol lipase catalyzes a reaction that uses water molecules to break the glycerol monoesters of long-chain fatty ... Monoacylglycerol+lipases at the U.S. National Library of Medicine Medical Subject Headings (MeSH) EC 3.1.1.23 Monoglyceride ... Monoacylglycerol lipase is a key enzyme in the hydrolysis of the endocannabinoid 2-arachidonoylglycerol (2-AG). It converts ...
... , together with gastric lipase, comprise the two acidic lipases. Lingual lipase uses a catalytic triad consisting ... Lingual lipase is a member of a family of digestive enzymes called triacylglycerol lipases, EC 3.1.1.3, that use the catalytic ... of total lipase activity in duodenum. This can be attributed to the fact that lingual lipase has a low pH optimum and can thus ... which can be attributed to low pancreatic lipase activity. Furthermore, milk fat is not a good substrate for pancreatic lipase ...
... is a form of lipase which functions intracellularly, in the lysosomes. The primary function of lysosomal ... Chlorpromazine is an inhibitor of lysosomal lipase. A genome wide survey suggests that lysosomal lipase A (located at ... lysosomal+acid+lipase,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH) v t e (Articles with ... Lysosomal lipases function optimally at an acidic pH which are complementary with the environment found in the lysosomal lumen ...
... (LIPG) is a form of lipase secreted by vascular endothelial cells in tissues with high metabolic rates and ... Endothelial lipase is secreted from vascular endothelial cells, being the only lipase to date. The primary secretion is that of ... Endothelial lipase is a protein that belongs triglyceride lipase category. This protein is encoded by the LIPG gene. ... Unlike the lipases that hydrolyze Triglycerides, endothelial lipase primarily hydrolyzes phospholipids. Due to the hydrolysis ...
"Entrez Gene: LIPE lipase, hormone-sensitive". Kraemer FB, Shen WJ (October 2002). "Hormone-sensitive lipase: control of ... Hormone-sensitive lipase (EC 3.1.1.79, HSL), also previously known as cholesteryl ester hydrolase (CEH), sometimes referred to ... Hormone-Sensitive+Lipase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) (CS1 errors: missing ... Although Hormone-Sensitive Lipase (HSL) is able to catalyze hydrolysis of triglycerides and diglycerides, another enzyme found ...
... is a genetic disorder in which a person has a defective gene for lipoprotein lipase, which leads ... More than 220 mutations in the LPL gene have been found to cause familial lipoprotein lipase deficiency so far.[citation needed ... "Familial lipoprotein lipase deficiency: MedlinePlus Medical Encyclopedia". medlineplus.gov. Retrieved 17 April 2019. Burnett, ... Familial lipoprotein lipase deficiency. Retrieved October 15, 2012. {{cite book}}: ,work= ignored (help) Gaudet, D; de Wal, J; ...
These lipases are closely related to each other and to lipoprotein lipase (EC 3.1.1.34), which hydrolyses triglycerides of ... Triglyceride lipases (EC 3.1.1.3) are a family of lipolytic enzymes that hydrolyse ester linkages of triglycerides. Lipases are ... Pancreatic lipase, also known as pancreatic triacylglycerol lipase or steapsin, is an enzyme secreted from the pancreas. As the ... Freie AB, Ferrato F, Carrière F, Lowe ME (2006). "Val-407 and Ile-408 in the beta5'-loop of pancreatic lipase mediate lipase- ...
... occurs when the enzyme lysosomal acid lipase that is needed to break down certain fats that are normally ... In acid lipase disease the lysosomal acid lipase enzyme is either lacking or missing. In both CESD and Wolman's disease there ... "lysosomal acid lipase deficiency , Counsyl". Counsyl. Retrieved 2017-11-08. NINDS. Acid Lipase Disease Information Page (All ... Three rare lipid storage diseases are caused by the deficiency of the enzyme lysosomal acid lipase: Lysosomal acid lipase ...
June 2020). "Adipose Triglyceride Lipase Is a Key Lipase for the Mobilization of Lipid Droplets in Human β-Cells and Critical ... June 2007). "Comparative studies of the role of hormone-sensitive lipase and adipose triglyceride lipase in human fat cell ... June 2007). "Adipose triglyceride lipase and hormone-sensitive lipase protein expression is decreased in the obese insulin- ... Adipose triglyceride lipase, also known as patatin-like phospholipase domain-containing protein 2 and ATGL, is an enzyme that ...
Lipase family member N is a protein that in humans is encoded by the LIPN gene. The gene encodes a lipase that is highly ... "Entrez Gene: Lipase family member N". Retrieved 2019-12-02. v t e This article incorporates text from the United States ...
Triacylglycerol lipase can refer to: Triacylglycerol lipase pancreatic lipase gastric lipase lingual lipase This disambiguation ... page lists articles associated with the title Triacylglycerol lipase. If an internal link led you here, you may wish to change ...
National Organization for Rare Disorders (NORD) Article - LYSOSOMAL ACID LIPASE/NIH.gov Article - LYSOSOMAL ACID LIPASE ... Lysosomal acid lipase deficiencies occur when a person has defects (mutations) in both copies of the LIPA gene. Each parent of ... Lysosomal acid lipase deficiency is a genetic disease that is autosomal recessive. It is an inborn error of metabolism that ... Lysosomal acid lipase deficiency (LAL deficiency or LAL-D) is an autosomal recessive inborn error of metabolism that results in ...
... (or BSDL), also known as carboxyl ester lipase (or CEL) is an enzyme produced by the adult pancreas ... "Effect of pancreatic phospholipase A2 and gastric lipase on the action of pancreatic carboxyl ester lipase against lipid ... Bile salt-stimulated lipase (or BSSL) is an equivalent enzyme found within breast milk. BSDL has been found in the pancreatic ... 1991). "Carboxyl ester lipase: a highly polymorphic locus on human chromosome 9qter". Genomics. 10 (2): 425-31. doi:10.1016/ ...
... is a protein that in humans is encoded by the LIPA gene. This gene encodes lipase A, the ... "Entrez Gene: Lipase A, lysosomal acid type". Retrieved 2018-08-22. Riemenschneider M, Mahmoodzadeh S, Eisele T, Klopp N, ... Wang F, Wang W, Wähälä K, Adlercreutz H, Ikonen E, Tikkanen MJ (December 2008). "Role of lysosomal acid lipase in the ... von Trotha KT, Heun R, Schmitz S, Lütjohann D, Maier W, Kölsch H (July 2006). "Influence of lysosomal acid lipase polymorphisms ...
"Physiology of Gastrointestinal Lipolysis and Therapeutical Use of Lipases and Digestive Lipase Inhibitors". Lipases and ... The pancreatic lipase is secreted to the small intestine where it is most active, at pH 7-7,5. Pancreatic lipase hydrolyses ... Gastric- and lingual lipases are the two acidic lipolytic enzymes that origin preduodenal but the gastric lipase is in much ... The pancreatic lipase consists of 465 amino acids. Schematic picture of pancreatic lipase is shown in figure 2. Pancreatic and ...
Osório, N. M.; Dubreucq, E.; Da Fonseca, MM R.; Ferreira-Dias, S. (2009), "Operational Stability of Immobilized Lipase/ ... Enzymes most suitable for this process are esterase; lipase; acylase; those enzymes that facilitate acidolysis reactions, ... Factors Influencing the Choice of Support for Immobilized Lipase.", Enzyme and Microbial Technology, 6 (10): 443-446, doi: ...
An increase in lipase activity has been reported in barley by MacLeod and White (1962), as cited by Chavan and Kadam (1989). ... Barley Lipase". Journal of the Institute of Brewing. 68 (6): 487-495. doi:10.1002/j.2050-0416.1962.tb01894.x. Shipard, Isabell ...
... amylase and lipase. A similar mixture of enzymes is sold as pancrelipase, which contains more active lipase enzyme than does ... Due to this association a maximum dose of 10,000 IU of lipase per kilogram per day is recommended. Though never reported there ... It is composed of amylase, lipase and protease. This mixture is used to treat conditions in which pancreatic secretions are ... "Pancrelipase Amylase; Pancrelipase Lipase; Pancrelipase Protease - Drug Usage Statistics". ClinCalc. Retrieved 7 October 2022. ...
Svendsen A (2000). "Lipase protein engineering". Biochim Biophys Acta. 1543 (2): 223-228. doi:10.1016/S0167-4838(00)00239-9. ... Some examples of degradative enzymes: Lipase, which digests lipids, Carbohydrases, which digest carbohydrates (e.g., sugars), ...
The degradation of triacylglycerides by hormone-sensitive lipase produces free fatty acids that are eventually converted to ... Kraemer, Fredric B.; Shen, Wen-Jun (2002). "Hormone-sensitive lipase". Journal of Lipid Research. 43 (10): 1585-1594. doi: ... a condition called ketoacidosis may develop because decreased insulin levels increase the activity of hormone sensitive lipase ...
APOE Lipoprotein lipase deficiency; 238600; LPL Lissencephaly 3; 611603; TUBA1A Lissencephaly syndrome, Norman-Roberts type; ... TP63 Lipase deficiency, combined; 246650; LMF1 Lipodystrophy, congenital generalized, type 1; 608594; AGPAT2 Lipodystrophy, ...
"triacylglycerol lipase - Homo sapiens". BRENDA. Technische Universität Braunschweig. Retrieved 25 May 2015. Tilg H, Moschen AR ... In humans, the butyrate precursor tributyrin, which is naturally present in butter, is metabolized by triacylglycerol lipase ...
... lipases; xylanases; pectinases; chitinases and their metabolites, including: 2-phenylamine; carotenoids; siderophores; cholic ...
  • citation needed] Lipase assist in the breakdown of fats in those undergoing pancreatic enzyme replacement therapy (PERT). (wikipedia.org)
  • For example, human pancreatic lipase (HPL), converts triglyceride substrates found in ingested oils to monoglycerides and two fatty acids. (wikipedia.org)
  • Pancreatic Lipase " has 1 results in Products. (rndsystems.com)
  • Pancreatic Lipase, also designated as pancreatic triacylglycerol acyl hydrolase, PL or PTL belongs to AB hydrolase superfamily. (biogenex.com)
  • Pancreatic Lipase hydrolyses insoluble, emulsified triglycerides into diglycerides, monoglycerides and free fatty acids in the intestine. (biogenex.com)
  • Low pancreatic lipase in insulin-dependent diabetics. (bmj.com)
  • Provides a "normal" or "abnormal" result for pancreatic lipase levels in just 10 minutes. (idexx.com.au)
  • Infiltration of porcine pancreatic lipase into magnetic hierarchical mesoporous UiO-66-NH 2 metal-organic frameworks for efficient detoxification of patulin from apple juice. (bvsalud.org)
  • This mesoporous structure (centered at 4.25 nm) allowed porcine pancreatic lipase (PPL) to infiltrate into the MOF shell at an immobilized amount of 255 mg/g, providing protection for PPL and enabling rapid separation and recovery. (bvsalud.org)
  • In the example of lysosomal lipase, the enzyme is confined within an organelle called the lysosome. (wikipedia.org)
  • Lipase is a protein ( enzyme ) released by the pancreas into the small intestine. (medlineplus.gov)
  • A deletion in the gene encoding hormone-sensitive lipase, a key enzyme for lipolysis, was associated with abnormalities in adipocyte function and systemic lipid and glucose homeostasis. (medpagetoday.com)
  • Lipase (LIE-pace) is an enzyme made by the pancreas that helps the body digest fats. (akronchildrens.org)
  • The disease is due to mutations in the gene LIPA (10q23.2-q23.3) encoding the enzyme lysosomal acid lipase (LAL). (orpha.net)
  • Lysosomal acid lipase deficiency (LAL-D), also known as Wolman disease or cholesterol ester storage disease (CESD), is an inherited genetic condition in which the body does not produce enough lysosomal acid lipase enzyme to process fats and cholesterol. (panfoundation.org)
  • Lipase is the type of enzyme that is specialized in breaking down fat. (enzymedica.com)
  • We then confirmed that geh was required for lipase activity and both forms of the purified enzyme had lipase activity. (uwo.ca)
  • The Lipase test measures the amount of Lipase, an enzyme produced by the pancreas , in the blood. (requestatest.com)
  • The HSL diacylglycerol lipase activity was inhibited by 98% upon incubation with anti-rat HSL antiserum, and the specific activity of chicken HSL was estimated to be approximately the same as for the rat enzyme. (lu.se)
  • Loss of the LD-associated Adipose Triglyceride Lipase (ATGL) disrupts both actin bundle formation and cortical actin integrity, an unusual phenotype also seen when Pxt, the enzyme responsible for prostaglandin (PG) synthesis, is missing. (biorxiv.org)
  • In a study of Old Order Amish patients, a mutation in the gene that encodes for hormone-sensitive lipase (HSL) was tied to dyslipidemia, hepatic steatosis, systemic insulin resistance, and diabetes, Coleen Damcott, PhD , of the University of Maryland School of Medicine in Baltimore, and colleagues reported online first in the New England Journal of Medicine . (medpagetoday.com)
  • Lipase (/ˈlaɪpeɪs, ˈlaɪpeɪz/ LY-payss, LY-payz) is a family of enzymes that catalyzes the hydrolysis of fats. (wikipedia.org)
  • A diverse array of genetically distinct lipase enzymes are found in nature, and they represent several types of protein folds and catalytic mechanisms. (wikipedia.org)
  • Other lipase enzymes, such as pancreatic lipases, are secreted into extracellular spaces where they serve to process dietary lipids into more simple forms that can be more easily absorbed and transported throughout the body. (wikipedia.org)
  • Dublin, Aug. 07, 2023 (GLOBE NEWSWIRE) -- The "Global Lipase Food Enzymes Markets, 2023-2029" report has been added to ResearchAndMarkets.com's offering. (globenewswire.com)
  • The global lipase food enzymes market is projected to witness substantial growth, reaching a market size of $679.5 million by 2029. (globenewswire.com)
  • Lipase enzymes play a crucial role in breaking down oils and fats into their basic components, such as fatty acids and glycerol. (globenewswire.com)
  • In the food industry, lipase enzymes are commonly used as additives to create a variety of food products. (globenewswire.com)
  • Food enzymes, including lipase, offer various functional qualities and can emulsify different food components, enhancing the kinetic stability of food. (globenewswire.com)
  • Moreover, lipase enzymes have the advantage of being considered clean-label ingredients, aligning with the growing demand for cleaner and more natural food products. (globenewswire.com)
  • Lipase enzymes find applications in various industries, including medicine and diagnostics. (globenewswire.com)
  • The rising consumption of processed foods and meat, along with increased awareness of animal health, is further propelling the demand for lipase enzymes. (globenewswire.com)
  • Overall, the global lipase food enzymes market is witnessing steady growth, driven by their diverse applications, biosensor technology, and the increasing demand for cleaner and healthier food products. (globenewswire.com)
  • Other enzymes and lipases from other microorganisms were also tested in the biocatalytic esterification of mono-and disaccharides. (researchgate.net)
  • Read on to learn more about types of lipase, enzymes for fat digestion and how to get help digesting all the fatty foods you love. (enzymedica.com)
  • Lipase enzymes help break down lipids and fats into molecules that are small enough to be absorbed into the blood. (enzymedica.com)
  • When you don't have enough lipase enzymes, it's like your body doesn't know what to do with these nutrients. (enzymedica.com)
  • Classically, lipases catalyse the hydrolysis of triglycerides: triglyceride + H2O → fatty acid + diacylglycerol diacylglycerol + H2O → fatty acid + monacylglycerol monacylglycerol + H2O → fatty acid + glycerol Lipases are serine hydrolases, i.e. they function by transesterification generating an acyl serine intermediate. (wikipedia.org)
  • Lipases are involved in diverse biological processes which range from routine metabolism of dietary triglycerides to cell signaling and inflammation. (wikipedia.org)
  • The ester hydrolysis activity of lipases has been well evaluated for the conversion of triglycerides into biofuels or their precursors. (wikipedia.org)
  • Background: Lipoprotein lipase (LPL) hydrolyzes triglycerides in plasma lipoproteins and enables uptake of lipolysis products for energy production or storage in tissues. (columbia.edu)
  • Lipase catalyzes hydrolysis of triglycerides to produce fatty acids and glycerol. (medscape.com)
  • Alpha toxin Pathology Lysosomal acid lipase deficiency Peripheral membrane proteins Phospholipase A Phospholipase C Triglyceride lipase Phospholipase A2 Outer membrane phospholipase A1 Patatin-like phospholipase Lombardo, Dominique (2001). (wikipedia.org)
  • A rare, progressive metabolic liver disease due to marked to complete lysosomal acid lipase deficiency and characterized by dyslipidemia and massive lipid accumulation leading to hepatomegaly and liver dysfunction, splenomegaly, accelerated atherosclerosis. (orpha.net)
  • Blood tests for lipase may be used to help investigate and diagnose acute pancreatitis and other disorders of the pancreas. (wikipedia.org)
  • Serum lipase levels in nonpancreatic abdominal pain versus acute pancreatitis. (springer.com)
  • Evaluation of amylase and lipase in the diagnosis of acute pancreatitis. (springer.com)
  • Lankisch PG, Burchard-Reckert S, Lehnick D. Underestimation of acute pancreatitis: patients with only a small increase in amylase/lipase levels can also have or develop severe acute pancreatitis. (springer.com)
  • Serum lipase and amylase are biochemical analyses used to establish the diagnosis of acute pancreatitis (AP). (scielo.org.za)
  • In the diagnosis of acute pancreatitis (AP), serum amylase and more recently lipase are the commonly used laboratory tests available to clinicians in South Africa (SA). (scielo.org.za)
  • Objective Serum lipase activities above the threefold upper reference limit indicate acute pancreatitis. (bmj.com)
  • Lipase testing is indicated in acute pancreatitis, as well as in the diagnosis of peritonitis, strangulated or infarcted bowel, and pancreatic cyst. (medscape.com)
  • Lipase testing is indicated in acute pancreatitis. (medscape.com)
  • Nevertheless, serum amylase and lipase are considered important tests in the diagnosis of acute pancreatitis. (medscape.com)
  • Serum lipase is a more reliable diagnostic marker of acute pancreatitis than serum amylase. (medscape.com)
  • The oil palm fruit mesocarp contains high lipase activity that increases free fatty acids and necessitates post-harvest inactivation by heat treatment of fruit bunches. (nature.com)
  • We investigated whether high lipase activity-within the reference range and in the absence of pancreatitis-are associated with genetic single nucleotide polymorphisms (SNP), and whether these identified SNPs are also associated with clinical pancreatitis. (bmj.com)
  • p=7.29×10 −8 ) with high lipase activity levels. (bmj.com)
  • This test may also be done for familial lipoprotein lipase deficiency . (medlineplus.gov)
  • Use the only pet-side test to measure feline pancreas-specific lipase levels. (idexx.com.au)
  • Malassezia globosa, a fungus thought to be the cause of human dandruff, uses lipase to break down sebum into oleic acid and increase skin cell production, causing dandruff. (wikipedia.org)
  • Today, the U.S. Food and Drug Administration approved Kanuma (sebelipase alfa) as the first treatment for patients with a rare disease known as lysosomal acid lipase (LAL) deficiency. (news-medical.net)
  • With a very high molar proportion of fatty acid to saccharide when compared to the other studies, the authors suggested that increasing the proportion of fatty acid could negatively affect the lipase conformation due to an acidification of the reaction medium. (researchgate.net)
  • Investigated were the catalytic activities and kinetics of lipases that were pretreated with carboxylic acids for the solvent-free esterification of propionic acid with isoamyl alcohol. (srce.hr)
  • From the kinetic analysis, the imprinting of lipases mainly enhanced the catalytic reaction rate constant rather than the affinity between lipase and propionic acid compared with untreated lipase. (srce.hr)
  • Lipase aids in digestion by helping to breakdown dietary fats. (requestatest.com)
  • Do low lipase & amylase levels indicate a health issue? (healthtap.com)
  • [7] Of the two non-clinical criteria for a diagnosis of AP, in terms of convenience and cost-containment it would be logical to favour the laboratory test ahead of the computed tomography (CT) scan, provided that reliance can be placed on the accuracy of serum lipase or amylase levels. (scielo.org.za)
  • Most lipases act at a specific position on the glycerol backbone of a lipid substrate (A1, A2 or A3). (wikipedia.org)
  • Lipases catalyze the hydrolysis of triacylglycerol to different glycerol derivatives and free fatty acids. (novozymes.com)
  • Antimicrobial lipids inhibit S. aureus growth and induce the staphylococcal proteolytic cascade, producing aureolysin (Aur) which processes the lipase glycerol ester hydrolase (Geh). (uwo.ca)
  • Human adipose tissue lipoprotein lipase (LPL) is stimulated in vivo by an insulin-glucose infusion. (diabetesjournals.org)
  • The replacement of chemical catalysts by lipases presents great benefits in terms of the nutritional properties of the obtained products and environmental care. (ejbiotechnology.info)
  • Lipases are catalysts for hydrolysis of esters and are useful outside of the cell, a testament to their wide substrate scope and ruggedness. (wikipedia.org)
  • With impressive substrate selectivity and fast reaction rates, lipases are excellent catalysts offering both a sustainable and cost-efficient alternative in your manufacturing. (novozymes.com)
  • Examples of commercial applications, where lipases are being deployed as catalysts are illustrated below. (novozymes.com)
  • Lipases perform essential roles in digestion, transport and processing of dietary lipids in most, if not all, organisms. (wikipedia.org)
  • In particular, Candida albicans has many lipases, possibly reflecting broad-lipolytic activity, which may contribute to the persistence and virulence of C. albicans in human tissue. (wikipedia.org)
  • In the present study, immobilisation of Candida rugosa (CRL) lipase onto amino-activated mica is performed via covalent bonding (namely Amino-CRL) and the cross-linking of lipases into nano-reactors through physical adsorption (namely NER-CRL). (researchgate.net)
  • SDS-Page: Recombinant Human Lipase A Protein [H00003988-P01] - 12.5% SDS-PAGE Stained with Coomassie Blue. (novusbio.com)
  • ANGPTL3 regulates lipoprotein metabolism by inhibiting lipoprotein and endothelial lipases. (medscape.com)
  • Karsenti D, Bacq Y, Brechot J, Mariotte N, Vol S, Tichet J. Serum amylase and lipase activities in normal pregnancy: a prospective case-control study. (springer.com)
  • During the study period, 476 patients presented with acute upper or generalised abdominal pain and raised serum amylase and/or lipase values. (scielo.org.za)
  • Although the international literature has shown serum amylase to be a less sensitive and specific test for AP than serum lipase, [1-6] serum amylase remains the most popular first-line investigation for suspected AP owing to the perception that the test is less expensive. (scielo.org.za)
  • Diabetes mellitus is associated with a reduction of lipoprotein lipase (LPL) activity and development of hypertriglyceridemia. (jci.org)
  • Even before heat treatment the mesocarp lipase activity causes consequential oil losses and requires costly measures to limit free fatty acids quantities. (nature.com)
  • Lipase activity can hydrolyze 30% of the oil content within 5 min 10 and large-scale exploitation of oil palm became feasible only after Fickendey 12 found a century ago that the lipase could be inactivated by heat treatment of harvested bunches. (nature.com)
  • To limit acidity, the bunches must be harvested before they are overripe, heat-sterilized rapidly (ideally within 1 day) to inactivate lipase activity and processed immediately. (nature.com)
  • The highest lipase activity was obtained with sunflower oil (2.5 U mL -1 ) in four days. (scialert.net)
  • Methods Genome-wide association studies (GWAS) on phenotypes 'serum lipase activity' and 'high serum lipase activity' were conducted including 3966 German volunteers from the population-based Study-of-Health-in-Pomerania (SHIP). (bmj.com)
  • Results Initial discovery GWAS detected SNPs within or near genes encoding the ABO blood group specifying transferases A/B ( ABO ), Fucosyltransferase-2 ( FUT2 ), and Chymotrypsinogen-B2 ( CTRB2 ), to be significantly associated with lipase activity levels in asymptomatic subjects. (bmj.com)
  • Loss-of-function variants have been shown to increase lipase activity, leading to a reduction in lipid levels and in risk for atherosclerotic cardiovascular disease (ASCVD), with no apparent adverse effects. (medscape.com)
  • We identify the lipase and its gene cosegregates with the low-/high-lipase trait, providing breeders a marker to rapidly identify potent elite genitors and introgress the trait into major cultivars. (nature.com)
  • Free and immobilised lipases were tested for their esterification activities. (researchgate.net)
  • All of the reported lipases primarily catalyzed esterification of lactose at the C6hydroxyl position (Table 1). (researchgate.net)
  • Enzymatic Kinetics of Solvent-free Esterification with Bio-imprinted Lipase', Chemical and Biochemical Engineering Quarterly , 33(4), pp. 495-499. (srce.hr)
  • The bio-imprinting treatment of lipase is found to be very effective for the yield and kinetics in solvent-free esterification. (srce.hr)
  • Inhibiting 2-AG degradation with the monoacylglycerol lipase (MAGL) inhibitor JZL184 during inflammation results in desensitization of CB1Rs by eCBs that is reversed with Cmp101. (iasp-pain.org)
  • From a prospective dataset on patients with acute abdominal pain and raised serum lipase and/or amylase values, the sensitivity and specificity of serum lipase, amylase and the two in combination was calculated for the diagnosis of AP, as defined by the Atlanta criteria. (scielo.org.za)
  • Specificity was 92% for lipase and 93% for amylase. (scielo.org.za)
  • We aimed to investigate the relative performance of serum lipase and amylase at our institution, in terms of both specificity for AP and sensitivity for the diagnosis of AP at the proposed threshold of three times the ULN. (scielo.org.za)
  • Thus, some lipase activities are confined to specific compartments within cells while others work in extracellular spaces. (wikipedia.org)
  • Severity of disease does not correlate with the degree of elevations of amylase and/or lipase. (springer.com)
  • Here we demonstrate that elite low-lipase lines yield oil with substantially less free fatty acids than standard genotypes, allowing more flexibility for post-harvest fruit processing and extended ripening for increased yields. (nature.com)
  • The liquid segment dominated the market in 2022, as liquid lipase is preferred for milk fat hydrolysis and is used in flavor enhancers and coffee whiteners. (globenewswire.com)
  • Pancreatitis can occur with normal or mild degree of amylase and lipase elevations, and thus, cross-sectional imaging can be helpful. (springer.com)
  • Lipases are used in many industrial applications where the chemical transformations include enantioselective resolution of esters and amides. (novozymes.com)
  • Extending this work, immobilised lipases have novel capabilities in the synthesis of sugar esters. (researchgate.net)
  • Lipase is commonly ordered along with an Amylase blood test . (requestatest.com)
  • Fungi and bacteria may secrete lipases to facilitate nutrient absorption from the external medium (or in examples of pathogenic microbes, to promote invasion of a new host). (wikipedia.org)
  • Regulation of lipoprotein lipase in the diabetic rat. (jci.org)
  • Lipase displayed a sensitivity of 91% for AP, against 62% for amylase. (scielo.org.za)
  • Because of its sensitivity, lipase testing is not very useful in chronic pancreatitis or pancreatic cancer. (medscape.com)
  • They also imply that, even within the reference range, elevated lipase activities may indicate subclinical pancreatic injury in asymptomatic subjects. (bmj.com)
  • From January 2010 to July 2012 at Tygerberg Academic Hospital, Cape Town, South Africa, data were collected prospectively on all patients presenting to the surgical admissions unit with acute generalised or upper abdominal pain and initial raised serum lipase and/or amylase values. (scielo.org.za)
  • Inclusion criteria were acute generalised or upper abdominal pain of less than 5 days' duration, with or without radiation to the back, and a raised serum lipase and/ or amylase value. (scielo.org.za)
  • Although lipase is mostly found in the pancreas, serum levels may also increase in association with other intra-abdominal pathologies or renal insufficiency. (medscape.com)
  • Monoacylglycerol lipase protects the presynaptic cannabinoid 1 receptor from desensitization by endocannabinoids after persistent inflammation. (iasp-pain.org)