TY - JOUR. T1 - Lipase production by immobilized Candida rugosa cells. AU - Ferrer, Pau. AU - Solà, Carles. PY - 1992/9/1. Y1 - 1992/9/1. N2 - Immobilization of Candida rugosa cells on a solid support for extracellular lipase production has been explored. The use of Ca-alginate beads and of mixed matrix of polyurethane foam/Ca-alginate beads enabled us to operate a batch and a continuous four-phase fluidized bed bioreactor. Cells co-entrapped together with polyurethane into Ca-alginate did not show higher lipase production levels than the cells entrapped in Ca-alginate gels. The addition of gum arabic to the medium greatly enhanced lipase production without affecting the hydrodynamic operating conditions significantly. This fact demonstrates that the reactor system is limited in terms of organic substrate dispersion and direct contact with cells. © 1992 Springer-Verlag.. AB - Immobilization of Candida rugosa cells on a solid support for extracellular lipase production has been explored. The ...
TY - JOUR. T1 - Comparison of the effect of post-heparin and pre-heparin lipoprotein lipase and hepatic triglyceride lipase on remnant lipoprotein metabolism. AU - Shirakawa, Takashi. AU - Nakajima, Katsuyuki. AU - Shimomura, Younosuke. AU - Kobayashi, Junji. AU - Stanhope, Kimber. AU - Havel, Peter J. AU - Machida, Tetsuo. AU - Sumino, Hiroyuki. AU - Murakami, Masami. PY - 2015/2/2. Y1 - 2015/2/2. N2 - Background: A comparison of post-heparin and pre-heparin plasma lipoprotein lipase (LPL) and hepatic triglyceride lipase (HTGL) on the metabolism of remnant lipoproteins (RLPs) has not been reported yet. Methods: Healthy volunteers were injected with heparin for LPL and HTGL determination in the fasting (8:00) and postprandial (20:00) plasma on the same day. Plasma total cholesterol (TC), triglycerides (TG), LDL-C, HDL-C, small dense LDL (sdLDL)-C, remnant lipoprotein (RLP)-C, RLP-TG, the RLP-TG/RLP-C ratio, adiponectin and apoCIII were measured. Results: LPL activity and concentration in the ...
In a lipase investigation, Candida antarctica lipase B (CALB) are explored for enzyme catalytic promiscuity. Enzyme catalytic promiscuity is shown by enzymes catalyzing alternative catalytic transformations proceeding via different transition state structures than normal. CALB normally performs hydrolysis reactions by activating and coordinating carboxylic acid/ester substrates in an oxyanion hole prior to nucleophilic attack from an active-site serine resulting in acyl enzyme formation. The idea of utilizing the carbonyl activation oxyanion hole in the active-site of CALB to catalyze promiscuous reactions arose by combining catalytic and structural knowledge about the enzyme with chemical imagination. We choose to explore conjugate addition and direct epoxidation activities in CALB by combining molecular modeling and kinetic experiments. By quantum-chemical calculations, the investigated promiscuous reactions were shown to proceed via ordered reaction mechanisms that differ from the native ping ...
The synthetic gene of CalBsyn was previously constructed to encode Candida antarctica lipase B (CALB). Lipase of CalBsyn gene is slightly different from...
Reaction rates and selectivities were measured for transacylation of fatty acid esters in solvents catalysed by Candida antarctica lipase B and by cutinase from Humicola insolens. With these enzymes classical water-based enzymology can be expanded to many different solvents allowing large variations in interaction energies between the enzymes, the substrates and the surrounding. Further ,hydrolysis reactions catalysed by Bacillus subtilis esterase 2 were investigated.. Thermodynamics analyses revealed that the enzyme contribution to reaction rate acceleration compared to acid catalysis was purely entropic. On the other hand, studies of differences in activation entropy and enthalpy between enantiomers and between homologous esters showed that high substrate specificity was favoured by enthalpic stabilisation.. Solvent was found to have a profound effect on enzyme catalysis, affecting both reaction rate and selectivity. Differences in substrate solubility will impact enzyme specificity since ...
The structure and flexibility of Candida antarctica lipase B in water and five different organic solvent models was investigated using multiple molecular dynamics simulations to describe the effect of solvents on structure and dynamics. Interactions of the solvents with the protein and the distribution of water molecules at the protein surface were examined. The simulated structure was independent of the solvent, and had a low deviation from the crystal structure. However, the hydrophilic surface of CALB in non-polar solvents decreased by 10% in comparison to water, while the hydrophobic surface is slightly increased by 1%. There is a large influence on the flexibility depending on the dielectric constant of the solvent, with a high flexibility in water and a low flexibility in organic solvents. With decreasing dielectric constant, the number of surface bound water molecules significantly increased and a spanning water network with an increasing size was formed. The reduced flexibility of Candida
PMRs report on global Microbial Lipase market. The global market of Microbial Lipase is US$ xx Mn/Bn in 2018 with xx% CAGR from 2014 to 2018 and it is spectated to peg US$ xx Mn/Bn by the end of 2029 with a CAGR of xx% from 2019 to 2029. The Microbial Lipase market study analyzes the historic, current and future behavior of the Microbial Lipase market with the help of DROT analysis and Porters Five Forces analysis.. The Microbial Lipase market report has considered 2018 as the base year, 2014-2018 as the historic period and 2019-2029 as the forecast period. Important segments by product type covered in the report include product 1, product 2, product 3 and product 4. Key end uses analyzed in the research consist of end use 1, end use 2, end use 3 and end use 4.. Request Sample Report @ https://www.persistencemarketresearch.co/samples/31180. key players and products ...
Hepatic lipase, also called hepatic triglyceride lipase (HTGL) or LIPC (for lipase, hepatic), is a form of lipase, catalyzing the hydrolysis of fats. It is expressed in the liver and adrenal glands. One of the principal functions of hepatic lipase is to convert intermediate-density lipoprotein (IDL) to low-density lipoprotein (LDL). LIPC encodes hepatic triglyceride lipase (HTGL), which is expressed in liver. LIPC has the dual functions of triglyceride hydrolase and ligand/bridging factor for receptor-mediated lipoprotein uptake. Hepatic lipase deficiency is a rare, autosomal recessive disorder that results in elevated high density lipoprotein (HDL) cholesterol due to a mutation in the hepatic lipase gene. Clinical features are not well understood and there are no characteristic xanthomas. There is an association with a delay in atherosclerosis in an animal model. GRCh38: Ensembl release 89: ENSG00000166035 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000032207 - Ensembl, May 2017 ...
TY - JOUR. T1 - Effect of germinated brown rice extracts on pancreatic lipase, adipogenesis and lipolysis in 3T3-L1 adipocytes. AU - See Meng, Lim. AU - Goh, Yong Meng. AU - Kuan, Wen Bin. AU - Loh, Su Peng. PY - 2014/11/3. Y1 - 2014/11/3. N2 - Background: This study investigated anti-obesity effects of seven different solvent (n-hexane, toluene, dicholoromethane, ethyl acetate, absolute methanol, 80% methanol and deionized water) extracts of germinated brown rice (GBR) on pancreatic lipase activity, adipogenesis and lipolysis in 3T3-L1 adipocytes. Methods: GBR were extracted separately by employing different solvents with ultrasound-assisted. Pancreatic lipase activity was determined spectrophotometrically by measuring the hydrolysis of p-nitrophenyl butyrate (p-NPB) to p-nitrophenol at 405 nm. Adipogenesis and lipolysis were assayed in fully differentiated 3T3-L1 adipocytes by using Oil Red O staining and glycerol release measurement. Results: GBR extract using hexane showed the highest ...
The gene encoding lipase B from Candida antarctica (CalB) was expressed in Pichia pastoris after it was synthesized by the recursive PCR and cloned into the Pichia expression plasmid, pPICZαA. The CalB was successfully secreted in the recombinant P. pastoris strain X-33 with an apparent molecular weight of 34 kDa. For 140 h flask culture, the dry cell weight and the extracellular lipase activity reached at 5.4 g/l and 57.9 U/l toward p-nitrophenyl palmitate, respectively. When we performed the fed-batch fermentation using a methanol feeding strategy for 110 h, the dry cell weight and the extracellular lipase activity were increased to 135.7 g/l and 11,900 U/l; the CalB protein concentration was 1.18 g/l of culture supernatant. The characteristics of CalB recovered from the P. pastoris culture were compared with the commercial form of CalB produced in Aspergillus oryzae. The kinetic constants and specific activity, the effects of activity and stability on temperature and pH, the glycosylation extent,
The triglyceride lipase gene subfamily plays a central role in lipid and lipoprotein metabolism. There are three members of this subfamily: lipoprotein lipase, hepatic lipase, and endothelial lipase. Although these lipases are implicated in the pathophysiology of hyperlipidemia and atherosclerosis, their structures have not been fully solved. In the current study, we established homology models of these three lipases, and carried out analysis of their activity sites. In addition, we investigated the kinetic characteristics for the catalytic residues using a molecular dynamics simulation strategy. To elucidate the molecular interactions and determine potential key residues involved in the binding to lipase inhibitors, we analyzed the binding pockets and binding poses of known inhibitors of the three lipases. We identified the spatial consensus catalytic triad Ser-Asp-His, a characteristic motif in all three lipases. Furthermore, we found that the spatial characteristics of the binding pockets ...
DISCUSSION The essential role of oxygen in lipid metabolism and cell growth is well known. Moreover, lipase production by several microorganisms depends on the availability of oxygen. Although in most cases oxygen seems to favor lipase production, low levels of aeration have also been reported to increase production of the enzyme (Corzo and Revah, 1999). It is often difficult to distinguish the effects of changes in stirring speed from changes in air flow rate. Both DO concentration and OTR have been used to correlate rates of aerobic fermentation. The OTR, however, is not constant during fermentation, varying with time due to the change in DO in the fermentation medium. Thus, kLa values can be used to establish the relationship between OTR and lipase production (Elibol and Ozer, 2000). It was clearly observed that an increase in stirring speed, rather than air flow rate, resulted in the most pronounced increase in kLa, as expected for a mechanically stirred vessel. Maximum extracellular lipase ...
TY - JOUR. T1 - Optimization and Modeling of Process Parameters for Lipase Production by Bacillus brevis. AU - Rajendran, Aravindan. AU - Thangavelu, Viruthagiri. PY - 2012/1/1. Y1 - 2012/1/1. N2 - Statistical evaluation of fermentation conditions and nutritional factors by Plackett-Burman two-level factorial design followed by optimization of significant parameters using response surface methodology for lipase production by Bacillus brevis was performed in submerged batch fermentation. Temperature, glucose, and olive oil were found to be the significant factors affecting lipase production. Maximum lipase activity of 5.1 U ml -1 and cell mass of 1.82 g l -1 at 32 h were obtained at the optimized conditions of temperature, 33.7 °C; initial pH, 8; and speed of agitation, 100 rpm, with the medium components: olive oil, 13.73 ml l -1; glucose, 13.98 g l -1; peptone, 2 g l -1; Tween 80, 5 ml l -1; NaCl, 5 g l -1; CH 3COONa, 5 g l -1; KCl, 2 g l -1; CaCl 2·2H 2O, 1 g l -1; MnSO 4·H 2O, 0. 5 g l -1; ...
TY - JOUR. T1 - A hybrid neural model (HNM) for the on-line monitoring of lipase production by Candida rugosa. AU - Boareto, Álvaro J.M.. AU - De Souza, Maurício B.. AU - Valero, Francisco. AU - Valdman, Belkis. PY - 2007/3/1. Y1 - 2007/3/1. N2 - A mechanistic model was proposed by Gordillo for the representation of lipase production by Candida rugosa, with the bioreactor in batch and fed-batch operation. However, the model was not able to represent the lipolytic activity. The objective of the present study is to propose an efficient hybrid neural-phenomenological model (HNM) for this process. The experimental data used corresponded to fed-batch operation with constant substrate feed rate at 2.8 × 10-7; 5.6 × 10-7 and 9.7 × 10-7 kg s-1. Artificial neural networks (ANNs) were trained to represent the aqueous and intracellular lipase activity and were further associated with a reduced version of the mechanistic model of the proposed HNM. When compared to the experimental data, the HNM ...
Lipases (triacylglycerol hydrolases) are hydrolytic enzymes that can catalyze the hydrolysis of the ester bond of long-chain acylglycerols at the oil-water interface. The present study investigated the effects of inducers, surface-active materials, activators, and inhibitors in the fermentation medium on lipase activity in Rhizopus delemar. In the presence of certain commercial oils and tributyrin as an inducer, lipase activity decreased in the order of sunflower oil > soybean oil > hazelnut oil > corn oil > tributyrin > olive oil. In addition, the effects of the stirring and aeration rates on lipase activity were investigated. To investigate the effect of surface-active materials on lipase activity 2 different surface-active materials, Tween-80 and rhamnolipid (biosurfactant), were used as comparatives with tributyrin. Maximum lipase activity was observed in the fermentation medium containing Tween-80 as both an inducer and surface-active material. The combined effects of molasses and sucrose ...
Lipase inhibitors are substances used to reduce the activity of lipases found in the intestine. Lipases are secreted by the pancreas when fat is present. The primary role of lipase inhibitors is to decrease the gastrointestinal absorption of fats. Fats then tend to be excreted in feces rather than being absorbed to be used as a source of caloric energy, and this can result in weight loss in individuals. These inhibitors could be used for the treatment of obesity, which can subsequently lead to Type II diabetes and cardiovascular diseases if not managed. An example of a lipase inhibitor is orlistat. Lipase inhibitors may affect the amount of fat absorbed, yet they do not block the absorption of a particular type of fat. Likewise, lipase inhibitors are not absorbed into the bloodstream. Lipase inhibitors bind to lipase enzymes in the intestine, thus preventing the hydrolysis of dietary triglycerides into monoglycerides and fatty acids. This then reduces the absorption of dietary fat. Lipase ...
The bacterial thermoalkalophilic lipases optimally hydrolyze saturated fatty acids at elevated temperatures. They also have significant sequence homology with staphylococcal lipases, and both the thermoalkalophilic and staphylococcal lipases are grouped as the lipase family 1.5. We report here the first crystal structure of the lipase family 1.5, the structure of a thermoalkalophilic lipase from Bacillus stearothermophilus L1 (L1 lipase) determined at 2.0-? resolution. The structure is in a closed conformation, and the active site is buried under a long lid helix. Unexpectedly, the structure exhibits a zinc-binding site in an extra domain that accounts for the larger molecular size of the family 1.5 enzymes in comparison to other microbial lipases. The zinc-coordinated extra domain makes tight interactions with the loop extended from the C terminus of the lid helix, suggesting that the activation of the family 1.5 lipases may be regulated by the strength of the interactions. The unusually long ...
Enzymes For Leather Alkaline Lipase JZ, Parameters: Appearance :White Powder, Components : Alkaline Lipase and special additives,&#...
A thermophilic bacterium, Bacillus sp. strain L2 was isolated from a hot spring in Perak, Malaysia. An extracellular lipase activity was detected through plate and broth assays at 70 °C after 28 h of incubation. The L2 lipase production was growth dependent as revealed by a number of factors affecting the secretion of extracelullar lipase. As for nutritional factors, casamino acids, trehalose, Ca2+ and Tween 60 were found to be more effective for lipase production. The optimum physical condition for L2 lipase production was obtained at 70 °C after 28 h of cultivation time, at pH 7.0, 150 rpm of agitation rate and 1% of starting inoculum size. The activity staining of crude L2 lipase revealed a clearing zone at 39 kDa. ...
Enzyme-linked immunoassay of mouse pancreatic lipase (PL) Kit instruction manual This reagent is for research purposes only: this kit is used to determine the activity of pancreatic lipase (PL) in mouse serum, plasma and related liquid samples. Experimental principle: This kit uses the double antibody sandwich method to determine the level of mouse pancreatic lipase (PL) in the specimen. Microporous plates were coated with purified pancreatic lipase (PL) antibody to prepare solid-phase antibodies. Pancreatic lipase (PL) was added to the monoclonal antibody-coated microwells, followed by HRP labeled pancreatic lipase (PL) antibody The combination forms an antibody-antigen-enzyme-labeled antibody complex. After thorough washing, the substrate TMB is added for color development. TMB is converted into blue under the catalysis of HRP enzyme, and into the final yellow under the action of acid. The color depth is positively correlated with pancreatic lipase (PL) in the sample. The absorbance (OD value) ...
The influence of water on the kinetics of alcoholysis of methyl propionate and n-propanol catalyzed by immobilized lipase B from Candida antarctica was studied in a continuous solid/gas reactor. In this reactor, the solid phase is composed of a packed enzymatic sample which is percolated by gaseous nitrogen, simultaneously carrying gaseous substrates to the enzyme while removing reaction products. In this system, interactions between the enzyme and non-reacting molecules are avoided, since no solvent is present, and it is thus more easy to assess the role of water. To this end, alcohol inhibition constant, substrates dissociation constants as well as acylation rate constant and ratio of acylation to deacylation rate constants have been determined as a function of water activity (aW). Data obtained highlight that n-propanol inhibition constant and dissociation constant of methyl propionate are a lot affected by aW variations whereas water has no significant effect on the catalytic acylation step nor on
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TY - ADVS. T1 - Integrated processing by magnetic separation technology for the multiple reuse of Candida antarctica lipase enzymes immobilised on magnetic micro particles. A2 - Schultz, Nadja. A2 - Hobley, Timothy John. A2 - Franzreb, Matthias. A2 - Syldatk, Christoph. N1 - Conference code: 6. PY - 2006. Y1 - 2006. M3 - Sound/Visual production (digital). T2 - 6th European Symposium on Biochemical Engineering Science. Y2 - 27 August 2006 through 30 August 2006. ER - ...
TY - JOUR. T1 - A case of non-alcoholic steatohepatitis complicated with severe acute pancreatitis induced by decreased lipoprotein lipase and hepatic triglyceride lipase activity levels in a young Japanese woman. AU - Minohara, Sawa. AU - Bae, Sung Kwan. AU - Sugiyama, Saori. AU - Shibata, Noriko. AU - Gushima, Toshifumi. AU - Motoshita, Junichi. AU - Shimoda, Shinji. AU - Takagi, Atsuko. AU - Ikeda, Yasuyuki. AU - Takahashi, Kazuhiro. PY - 2018/9. Y1 - 2018/9. N2 - We report a case of non-alcoholic steatohepatitis complicated with acute pancreatitis induced by hypertriglyceridemia in a young Japanese woman. A precise examination of the lipid profile showed decreased lipoprotein lipase (LPL) and hepatic triglyceride lipase activity levels, while the LPL mass was at the minimum level of the normal range.. AB - We report a case of non-alcoholic steatohepatitis complicated with acute pancreatitis induced by hypertriglyceridemia in a young Japanese woman. A precise examination of the lipid profile ...
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TY - JOUR. T1 - The crystal structure of a triacylglycerol lipase from Pseudomonas cepacia reveals a highly open conformation in the absence of a bound inhibitor. AU - Kim, Kyeong Kyu. AU - Song, Hyun Kyu. AU - Shin, Dong Hae. AU - Hwang, Kwang Yeon. AU - Sun, Se Won. PY - 1997/2/15. Y1 - 1997/2/15. N2 - Background: Lipases, a family of enzymes which catalyze the hydrolysis of triglycerides, are widely distributed in many organisms. True lipases are distinguished from esterases by the characteristic interfacial activation they exhibit at an oil-water interface. Lipases are one of the most frequently used biocatalysts for organic reactions performed under mild conditions. Their biotechnological applications include food and oil processing and the preparation of chiral intermediates for the synthesis of enantiomerically pure pharmaceuticals. Recent structural studies on several lipases have provided some clues towards understanding the mechanisms of hydrolytic activity, interfacial activation, and ...
The production of commercial enzymes, including lipase from bacteria has always been the industrial choice due to its economical and commercial feasibility. Lipases are produced by microorganisms such as bacteria and fungi. However, we have focused on bacterial microbial lipases were economically importance of several properties. The present studies of the goals of this paper were isolation and identification of lipase producing bacteria from Oil contaminated soil. Screening and isolation of lipase producing strains of bacteria was carried out from different soil samples collected from various area in Surat, Gujarat, India. Tributyrin agar, selective media for isolation of lipase producing bacteria was used. Out of 41 isolates,20 were showing lipolytic activity. Agar well diffusion method used for further screening of best isolate for lipase production. The isolate AD1 with maximum zone of 27mm on Phenol red agar plate produce the lipase with the activity of 4.27U/ml obtained after 96hrs of incubation
The synthesis of citronellyl butyrate by direct esterification reaction catalyzed by immobilized lipase from Candida rugosa was studied in a continuous packed bed reactor using n-hexane as organic solvent. Parameters such as residence time, temperature, and pH were examined. The optimum conversion was obtained at a flow rate of 1 ml/min (residence time 8 min), temperature of 50 °C, and pH 7.5. At high temperature, biocatalyst was rapidly deactivated with respect to time. The immobilized lipase was stable at pH range of 6 to 9. The deactivation of biocatalyst was increased at pH of immobilized lipase 4 and 10 in comparison with pH range from 5 to 9. The esterification reaction in packed-bed reactor was modeled by ping pong model and ping pong with product inhibition model. The observed kinetics behaviour of esterification reaction was found to follow a ping pong with product inhibition model. In this study, the conversion of butyric acid and stability of immobilized lipase was higher in the system with
Fat tissue is the most important energy depot in vertebrates. The release of free fatty acids (FFAs) from stored fat requires the enzymatic activity of lipases. We showed that genetic inactivation of adipose triglyceride lipase (ATGL) in mice increases adipose mass and leads to triacylglycerol deposition in multiple tissues. ATGL-deficient mice accumulated large amounts of lipid in the heart, causing cardiac dysfunction and premature death. Defective cold adaptation indicated that the enzyme provides FFAs to fuel thermogenesis. The reduced availability of ATGL-derived FFAs leads to increased glucose use, increased glucose tolerance, and increased insulin sensitivity. These results indicate that ATGL is rate limiting in the catabolism of cellular fat depots and plays an important role in energy homeostasis.. ...
The structural gene (lipA) coding for the extracellular lipase of Pseudomonas aeruginosa PAO1 has been cloned on plasmid pSW118. Nucleotide sequence analysis revealed a gene of 936 bp. lipA codes for a proenzyme of 311 amino acids including a leader sequence of 26 amino acids. The mature protein was predicted to have a M r of 30134, an isoelectric point of 5.6, and a consensus sequence (IGHSHGG) typical of lipases. Furthermore it is highly homologous (>60%) to other lipases from various pseudomonads. The lipA gene failed to hybridize detectably with genomic DNA from other Pseudomonas species except P. alcaligenes, even under relaxed stringency. Located 220 bp downstream of the lipA gene, is an open reading frame (ORF2, lipH) which encodes a hydrophilic protein (283 amino acids; M r 33587) that shows some homology to the limA gene product of P. cepacia. In complementation tests of lipase-defective mutants, lipH was shown to be necessary for expression of active extracellular lipase in P. aeruginosa
A novel lipase gene lip5 from the yeast Candida albicans was cloned and sequenced. Alignment of amino acid sequences revealed that 86-34% identity exists with lipases from other Candida species. The lipase and its mutants were expressed in the yeast Pichia pastoris, where alternative codon usage caused the mistranslation of 154-Ser and 293-Ser as leucine. 154-Ser to leucine resulted in loss of expression of Lip5, and 293-Ser to leucine caused a marked reduction in the lipase activity. Lip5-DM, which has double mutations that revert 154 and 293 to serine residues, showed good lipase activity, and was overexpressed and purified by (NH4)2SO4 precipitation and ion-exchange chromatography. The pure Lip5-DM was stable at low temperatures ranging from 15-35 °C and pH 5-9, with the optimal conditions being 15-25 °C and pH 5-6. The activation energy of recombinant lipase was 8.5 Kcal/mol between 5 and 25 °C, suggesting that Lip5-DM was a cold-active lipase. Its activity was found to increase in the presence
The principal objectives of this study were to evaluate the kinetics of lipase production by Staphylococcus warneri EX17 under different oxygen volumetric mass…
New Atglistatin closely related analogues: Synthesis and structure-activity relationship towards adipose triglyceride lipase inhibition
extracellular region, extracellular space, lipase activity, triglyceride lipase activity, lipid digestion, lipid metabolic process, positive regulation of triglyceride lipase activity, retinoid metabolic process
Endothelial lipase is a form of lipase secreted by vascular endothelial cells in tissues with high metabolic rates and vascularization, such as the liver, lung, kidney, and thyroid gland.[1] Unlike the lipases that hydrolyze triglycerides, endothelial lipase primarily hydrolyzes phospholipids.[1] It was first characterized in 1999.[2] ...
In the presence of taurodeoxycholate, cis-unsaturated fatty acids increase porcine pancreatic lipase activity 15-fold at pH 7.5. This effect is saturable with a low proportion of fatty acid to substrate. The overall angle of the fatty acid, the position of its double bond and the presence of a carbo …
The Lipase Engineering Database is online ! The Lipase Engineering Database (LED) is a WWW-accessible resource on sequence-structure-function relationships of microbial lipases. Sequences of 92 microbial lipases and homologous serine hydrolases were assigned to 32 homologous families and 15 superfamilies. Multisequence alignments of all homologous families and superfamilies are provided. Functionally relevant amino acids are annotated. The complete catalytic machinery (catalytic triad and two oxyanion hole residues) could be annotated in 91 % of LED sequence entries. Published mutants and their properties are provided. The X-ray structures of 22 lipases were superposed and annotated. Consistently annotated aligned sequences and superimposed structures of microbial lipases help to understand the functional role of individual amino acids and thus the LED is a useful tool for protein engineering. We have also set up a mailing list as a forum for discussions and announcements on topics related to ...
Introduction: Myocardial metabolism undergoes change in response to pathological cardiac hypertrophy (PH), characterized by increased reliance on glucose oxidation, decreased free fatty acid (FFA) oxidation and a loss of metabolic flexibility. Cardiac metabolism is influenced by other organs such as adipose tissue. Hence, we aimed to investigate the effect of Adipose Triglyceride Lipase (ATGL) in adipose tissue on the development of PH and heart failure (HF) in a pressure overload-induced cardiac hypertrophy model in mice.. Methods: Male adipose tissue specific ATGL-knock out (atATGL-KO) and wild type mice (WT) underwent sham surgery (sham) or transverse aortic constriction (TAC). After 11 weeks, mice were sacrificed and organs were harvested.. We performed echocardiography one week before and 11 weeks after surgery. Left ventricular mass (LVM), left ventricular mass/tibia length (LVM/TL) and ejection fraction (EF) were calculated. Beta-myosin heavy chain (β-MyHC) was measured in RNA of hearts. ...
Background. Serum lipase and amylase are biochemical analyses used to establish the diagnosis of acute pancreatitis (AP). Despite lipase having been shown internationally to be a more sensitive and specific test, amylase remains a popular first-line test. Objective. To provide a local basis for the recommendation of the best first-line laboratory test, an assessment of their performance in our local setting was undertaken. Methods. 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. Results. During the study period, 476 patients presented with acute upper or generalised abdominal pain and raised serum amylase and/or lipase values. The median age of the patients was 43 years (range 14 - 85), and 58% were men and 42% women. Of the patients, 322 (68%) presented with abdominal conditions
Creative Enzymes (US). The report begins with the overview of the Bacteria Sourced Microbial Lipase Market and offers throughout development. It presents a comprehensive analysis of all the regional and major player segments that gives closer insights upon present market conditions and future market opportunities along with drivers, trending segments, consumer behaviour, pricing factors and market performance and estimation throughout the forecast period.. The report also covers geographical markets and key players that have adopted significant strategies for business developments. The data within the report is displayed in a statistical format to offer a better understanding upon the dynamics. The report compiles exhaustive information acquired through proven research methodologies and from dedicated sources across several industries.. To Buy Full Version Of This Report, Visit https://dataintelo.com/checkout/?reportId=127302. The report segments the Global Bacteria Sourced Microbial Lipase ...
Phosphorylation of adipose triglyceride lipase Ser(404) is not related to 5-AMPK activation during moderate-intensity exercise in humans
TY - JOUR. T1 - Visceral obesity, hepatic lipase activity, and dyslipidemia in type 1 diabetes. AU - Sibley, Shalamar D.. AU - Palmer, Jerry P.. AU - Hirsch, Irl B.. AU - Brunzell, John D.. PY - 2003/7/1. Y1 - 2003/7/1. N2 - Excessive weight gain in a subset of intensively treated Diabetes Control and Complications Trial (DCCT) subjects was associated with higher waist to hip ratio; higher triglyceride (TG), low-density lipoprotein (LDL) cholesterol, and apolipoprotein B (ApoB) in the presence of small-dense LDL; and decreased high-density lipoprotein 2 cholesterol (HDL2-C), suggesting that weight gain in these subjects resulted in higher intraabdominal fat (IAF), and an atherosclerotic dyslipidemia mediated through hepatic lipase activity (HL). Objectives were to investigate relationships between IAF, HL, and dyslipidemia and to relate IAF to previous body mass index change during the DCCT. Sixty-one subjects were studied approximately 4 yr after DCCT closeout. IAF was positively related to HL ...
Pancreatic lipase is considered an important target for the control of hyperlipidemia. Several plants, especially those rich in phenolic metabolites, have been shown to have anti-hyperlipidemic activity and are considered a good alternative for obesity prevention. Extracts of the stem bark of Endopleura uchi (Huber) Cuatrec (Humiriaceae) were evaluated for the inhibitory activity on the pancreatic lipase enzyme, as well as their antioxidant potential were verified in the 2,2-diphenyl-1-picrylhydrazyl (DPPH) test. In addition, the total phenolics (TPC) and flavonoids contents (TFC) were estimated. In general way, the acetonic and ethanolic extracts showed better results than aqueous extract. At the concentration of 1 mg/mL, both acetonic and ethanolic extracts inhibited the activity of pancreatic lipase by 49.33 and 36.88%, representing 135.26 and 102.75 of inhibited lipase activity per gram of extract (ILA/g). On the other hand, the aqueous extract inhibited lipase by 47.54% at the concentration of 2
Enzyme selectivity means that the enzyme´s preferences towards competing substrates will be different. In this thesis, the enzyme selectivity has been studied for utilization in synthesis of functionalized macromonomers. The aim was to study how the inherent -or introduced - selectivity of lipases can be used to introduce thiol‐ or enefunctionalities into short polyesters. Thiol‐ and ene‐functionalized renewable organic precursor molecules in combination with thiol‐ene click chemistry opens up for a sustainable material production. Lipases do not normally affect ene‐moieties and the preference towards thiols is low, enabling introduction of these functional groups for further modifications. In addition, lipases have been shown to be good catalysts in the formation of polyesters, both via ring‐opening and polycondensation polymerization.. In paper I Candida antarctica lipase B was used to end‐functionalize poly(ε‐caprolactone) with free thiols in a one‐pot reaction. The ...
In nature, lipases (EC 3.1.1.3) catalyze the hydrolysis of triglycerides to form glycerol and fatty acids. Under the appropriate conditions, the reaction is reversible, and so biotechnological applications commonly make use of their capacity for esterification as well as for hydrolysis of a wide variety of compounds. In the present paper, we report the X-ray structure of lipase A from Candida antarctica, solved by single isomorphous replacement with anomalous scattering, and refined to 2.2-Å resolution. The structure is the first from a novel family of lipases. Contrary to previous predictions, the fold includes a well-defined lid as well as a classic α/β hydrolase domain. The catalytic triad is identified as Ser184, Asp334 and His366, which follow the sequential order considered to be characteristic of lipases; the serine lies within a typical nucleophilic elbow. Computer docking studies, as well as comparisons to related structures, place the carboxylate group of a fatty acid product near ...
At Biocatalysts we produced a panel of lipase enzymes based on the specificity of the oil substrate used for the hydrolysis reaction. We followed our Design for Manufacture (DFM) approach to ensure that any enzyme(s) selected had already been evaluated at the start of the project for its operational (high production yield and downstream processing) and regulatory requirements. The panel of new lipases was sent to Oleon for evaluation with the specific oil and one of the enzymes performed within the selected parameters.. Using Biocatalysts expert knowledge, this enzyme was scaled up to produce a more commercially representative sample of the enzyme via small scale fermentation and DSP processes (ensuring both processes are scalable and transferable to full scale manufacture of the enzyme). The larger sample produced was sent to Oleon for further testing for hydrolysis of the specific oil at laboratory scale (,100mL) and at small scale reactor level (,5L). Results from Oleon confirmed the new ...
TY - JOUR. T1 - Severe reduction of blood lysosomal acid lipase activity in cryptogenic cirrhosis. T2 - A nationwide multicentre cohort study. AU - Angelico, Francesco. AU - Corradini, Stefano Ginanni. AU - Pastori, Daniele. AU - Fargion, Silvia. AU - Fracanzani, Anna Ludovica. AU - Angelico, Mario. AU - Bolondi, Luigi. AU - Tozzi, Giulia. AU - Pujatti, Pietro Luigi. AU - Labbadia, Giancarlo. AU - Corazza, Gino Roberto. AU - Averna, Maurizio. AU - Perticone, Francesco. AU - Croce, Giuseppe. AU - Persico, Marcello. AU - Bucci, Tommaso. AU - Baratta, Francesco. AU - Polimeni, Licia. AU - Del Ben, Maria. AU - Violi, Francesco. PY - 2017/7/1. Y1 - 2017/7/1. N2 - Background and aims Blood lysosomal acid lipase (LAL) is reduced in non-alcoholic steatohepatitis, which is the major cause of cryptogenic cirrhosis (CC); few data on LAL activity in CC do exist. We investigated LAL activity in a cohort of patients with liver cirrhosis. Methods This is a multicentre cohort study including 274 patients with ...
Although the structure of Human Pancreatic Lipase has been documented through the X-ray crystallography, the knowledge about the molecular rearrangement and dynamic equilibrium in the structure (particularly in the catalytic triad and lid domains) is very scanty. The structural fluctuations and conformational changes undergo by Human Pancreatic Lipase (HPL) with and without colipase were computationally investigated through molecular dynamics simulation technique using GROMACS 2018.4, MOE 2016.0801 and VMD softwares in order to gain insight into the complex transitions at different domains. The structural stability was revealed vis-a-vis Root Mean Square Deviation (RMSD) and Root Mean Square Fluctuations (RMSF) plots. The levels of compactness/folding and conformational changes of the protein were determined using Radius of gyration and secondary analysis respectively. Salt bridge analysis gives more ionic pairs interactions than experimentally determined results. Results show that though both proteins
Title:Enzymatic Synthesis of Butyl Laurate by Immobilized Rhizopus Oryzae Lipase onto Silica Aerogel: Optimization by Response Surface Methodology. VOLUME: 7 ISSUE: 2. Author(s):Nadia Kharrat, Imen Aissa, Amel Kamoun, Yassine Ben Ali, Maha Chaâbouni-Karra and Youssef Gargouri. Affiliation:Laboratoire de Biochimie et de Génie Enzymatique des Lipases, ENIS route de Soukra, BP1173, University of Sfax, 3038 Sfax, Tunisia.. Keywords:Esterification of butyl laurate, Immobilized Rhizopus oryzae lipase, silica aerogel, Response surface methodology (RSM), Box-Behnken Design, Cosmetic and oleochemistry fields.. Abstract:Given the importance of butyl laurate in various industrial fields, its production by enzymatic catalysis has received greater interest. Butyl laurate was successfully synthesised by the esterification of lauric acid with butanol. This reaction was catalyzed by Rhizopus oryzae lipase immobilized onto silica aerogel in organic media. Response surface methodology was applied in order to ...
Lipase production by Geotrichum candidum NRRL Y‐552 was studied using an alternative nitrogen source, yeast hydrolysate (Prodex‐lac®), and soybean oil as the carbon source and inducer of lipase production. Factorial design and response surface methodologies were applied to obtain optimized conditions for lipase production in shaken flasks, defined as: 3.5 g/100 mL of yeast hydrolysate and 0.7 g/100 mL of soybean oil with an initial pH of 7.0 at 30 °C and 250 rpm. The resulting lipase activity after 48 h was 24.3 U/mL (0.506 U/mL.h), 52 % higher than with peptone under the same conditions (U = the amount of enzyme required to liberate 1 µmol of fatty acid per minute). Lipase production with the optimized medium was conducted in a stirred tank reactor and in an airlift bioreactor, both at 30 °C and 300 rpm; the best results obtained were 15.4 U/mL after 32 h of fermentation (0.481 U/mL.h) and 19.24 U/mL after 32 h of fermentation (0.601 U/mL.h) at 1 vvm, respectively. The results presented ...
TY - JOUR. T1 - Improvement in the secretory expression of recombinant Candida rugosa lipase in Pichia pastoris. AU - Kuo, Ting Chun. AU - Shaw, Jei Fu. AU - Lee, Guan Chiun. PY - 2015/12/1. Y1 - 2015/12/1. N2 - The yeast Candida rugosa can secrete a mixture of lipase isoenzymes (Lips), which have been widely applied in industry. Eight Lip genes (LIP1 to LIP8) have been identified and are expressed in Pichia pastoris. However, the expression level was not sufficient for economical industrial application. In this study, two combined processes of antibiotic selection and low-temperature culture efficiently elicited a high-level secretion of recombinant Lip2 in P. pastoris. The LIP2 gene copy number of the Pichia transformants was increased by sequential selections at gradually increasing Zeocin concentrations. After the first selection at 500 μg/mL of Zeocin, three clones (500-clones) with 2.4-fold to 5.8-fold improvement in Lip2 secretion were identified from 105 survival clones through lipase ...
The characteristic of most lipases is the interfacial activation at a lipid interface or in non-polar solvents. Interfacial activation is linked to a large conformational change of a lid, from a closed to an open conformation which makes the active site accessible for substrates. While for many lipases crystal structures of the closed and open conformation have been determined, the pathway of the conformational transition and possible bottlenecks are unknown. Therefore, molecular dynamics simulations of a closed homology model and an open crystal structure of Burkholderia cepacia lipase in water and toluene were performed to investigate the influence of solvents on structure, dynamics, and the conformational transition of the lid. The conformational transition of B. cepacia lipase was dependent on the solvent. In simulations of closed B. cepacia lipase in water no conformational transition was observed, while in three independent simulations of the closed lipase in toluene the lid gradually opened
Lipase maturation factor 1 (LMF1) is predicted to be a polytopic protein localized to the endoplasmic reticulum (ER) membrane. It functions in the post-translational attainment of enzyme activity for both lipoprotein lipase and hepatic lipase. By using transmembrane prediction methods in mouse and human orthologs, models of LMF1 topology were constructed and tested experimentally. Employing a tagging strategy that used insertion of ectopic glycan attachment sites and terminal fusions of green fluorescent protein, we established a five-transmembrane model, thus dividing LMF1 into six domains. Three domains were found to face the cytoplasm (the amino-terminal domain and loops B and D), and the other half was oriented to the ER lumen (loops A and C and the carboxyl-terminal domain). This representative model shows the arrangement of an evolutionarily conserved domain within LMF1 (DUF1222) that is essential to lipase maturation. DUF1222 comprises four of the six domains, with the two largest ones ...
A novel method for the assay of polyhydroxyalkanoate (PHA)-degrading ability of triacylglycerol lipases was developed. By applying the natural affinity of lipases towards hydrophobic interfaces, a sensitive and rapid densitometry analysis for the evaluation of hydrolytic activity of lipase droplets towards PHA-coated surface was successfully carried out. We found that 12 out of 14 tested lipases which are of fungal, bacterial and animal origin were able to hydrolyze P(3HB-co-92 mol% 4HB) thin film. The patterns and opacity of the hydrolysis spots of lipases on PHA films allowed easy comparison of PHA-hydrolytic strength of lipases. Lipase from the bacterium Chromobacterium viscosum exhibited the highest PHA-degrading activity. The hydrolytic activity of lipases on water insoluble PHA, emulsified p-nitrophenyl laurate and olive oil were also compared and interestingly some lipases showed better activity when PHA was used as a substrate.
TY - JOUR. T1 - Serum lipase activity in experimental acute hemorrhagic pancreatitis. AU - PERSKY, L.. AU - RAVIN, H. A.. AU - JACOB, S.. AU - SELIFMAN, A. M.. N1 - Copyright: Copyright 2018 Medline is the source for the citation and abstract of this record.. PY - 1951/8/1. Y1 - 1951/8/1. KW - BLOOD. KW - LIPASE. KW - PANCREATITIS. UR - http://www.scopus.com/inward/record.url?scp=76949121771&partnerID=8YFLogxK. UR - http://www.scopus.com/inward/citedby.url?scp=76949121771&partnerID=8YFLogxK. U2 - 10.1152/ajplegacy.1951.166.2.413. DO - 10.1152/ajplegacy.1951.166.2.413. M3 - Article. C2 - 14857195. AN - SCOPUS:76949121771. VL - 166. SP - 413. EP - 415. JO - The American journal of physiology. JF - The American journal of physiology. SN - 0002-9513. IS - 2. ER - ...
Buy our Recombinant Human Pancreatic Lipase Related Protein 2. Ab114929 is a protein fragment produced in Wheat germ and has been validated in WB, ELISA…
OBJECTIVE: Pigment epithelium-derived factor (PEDF) is an adipocyte-secreted factor involved in the development of insulin resistance in obesity. Previous studies have identified PEDF as a regulator of triacylglycerol metabolism in the liver that may act through adipose triglyceride lipase (ATGL). We used ATGL(-/-) mice to determine the role of PEDF in regulating lipid and glucose metabolism. RESEARCH DESIGN AND METHODS: Recombinant PEDF was administered to ATGL(-/-) and wild-type mice, and whole-body energy metabolism was studied by indirect calorimetry. Adipose tissue lipolysis and skeletal muscle fatty acid metabolism was determined in isolated tissue preparations. Muscle lipids were assessed by electrospray ionization-tandem mass spectrometry. Whole-body insulin sensitivity and skeletal muscle glucose uptake were assessed. RESULTS: PEDF impaired the capacity to adjust substrate selection, resulting in a delayed diurnal decline in the respiratory exchange ratio, and suppressed daily fatty ...
For a better understanding of the previously reported enantioselectivity of Pseudomonas cepacia lipase (PCL) in acylation of racemic primary alcohols, 2-methyl-3(or 4)-arylalkanols, molecular modeling of tetrahedral intermediates (TIs) at the active site was performed. The most probable conformers of TIs were elucidated and their interactions with the amino acid residues of the binding pockets at the enzyme active site were studied. The free energy difference between TIs of two enantiomers was approximated by the differences in potential energy and the solvent accesible surface area. Correlation between the HE(His286). . .O gamma (Ser87) hydrogen bond differences of diastereomeric, low energy gauche-TIs, and experimentally determined enantiomeric ratios was found. In agreement with the stereoelectronic theory, the gauche-TI precedes ester release.. ...
Introduction. Comparing the effect of different temperatures on free lipase and immobilised lipase Plan Lipase is an enzyme which hydrolyses fats to fatty acids and glycerol. Glycerol has three hydroxyl groups. Fatty acid molecules are much larger than glycerol molecules and consist of long hydrocarbon chains. Lipase works by hydrolysis, adding three molecules of water across the ester link. Hypothesis My hypothesis is that immobilised lipase will work more efficiently at high temperatures than free lipase. Free lipase is when lipase is prepared free in solution. It is used to digest fats as, for e.g., in some biological washing powders. It is also used in the food industry. Free lipase works best at temperatures of 30-50�C. However, when an enzyme is immobilised some of its physical properties are changed. There are three ways to immobilise enzymes. Entrapment is the gentlest method of immobilisation and does not damage enzymes. The enzymes are also more stable due to entrapment. The chief ...
TY - JOUR. T1 - The short form of the recombinant CAL-A-type lipase UM03410 from the smut fungus Ustilago maydis exhibits an inherent trans-fatty acid selectivity. AU - Brundiek, Henrike. AU - Saß, Stefan. AU - Evitt, Andrew. AU - Kourist, Robert. AU - Bornscheuer, Uwe T. N1 - Brundiek, Henrike Sass, Stefan Evitt, Andrew Kourist, Robert Bornscheuer, Uwe T Germany Applied microbiology and biotechnology Appl Microbiol Biotechnol. 2012 Apr;94(1):141-50. Epub 2012 Feb 1.. PY - 2012/4. Y1 - 2012/4. N2 - The Ustilago maydis lipase UM03410 belongs to the mostly unexplored Candida antarctica lipase (CAL-A) subfamily. The two lipases with [corrected] the highest identity are a lipase from Sporisorium reilianum and the prototypic CAL-A. In contrast to the other CAL-A-type lipases, this hypothetical U. maydis lipase is annotated to possess a prolonged N-terminus of unknown function. Here, we show for the first time the recombinant expression of two versions of lipase UM03410: the full-length form (lipUMf) ...
Three sub-group lipases of Burkholderia cepacia lipase (BCL), Rhizomucor miehei lipase (RML), and Candida rugosa lipase (CRL) were covalently immobilized on den
Visceral adipose tissue plays a critical role in numerous diseases. While imaging studies often show adipose involvement in abdominal diseases, their outcomes may vary from being a mild self limited illness to one with systemic inflammation and organ failure. We therefore compared the pattern of visceral adipose injury during acute pancreatitis and acute diverticulitis to determine its role in organ failure. Acute pancreatitis-associated adipose tissue had ongoing lipolysis in the absence of adipocyte triglyceride lipase (ATGL). Pancreatic lipase injection into mouse visceral adipose tissue hydrolyzed adipose triglyceride and generated excess non-esterified fatty acids (NEFA), which caused organ failure in the absence of acute pancreatitis. Pancreatic triglyceride lipase (PNLIP) increased in adipose tissue during pancreatitis and entered adipocytes by multiple mechanisms, hydrolyzing adipose triglyceride and generating excessive NEFA. During pancreatitis, obese PNLIP knockout mice, unlike obese ...
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Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, ...
Build: Wed Jun 21 18:33:50 EDT 2017 (commit: 4a3b2dc). National Center for Advancing Translational Sciences (NCATS), 6701 Democracy Boulevard, Bethesda MD 20892-4874 • 301-435-0888. ...
The integrity of the vascular barrier, which is essential to blood vessel homoeostasis, can be disrupted by a variety of soluble permeability factors during sepsis. Pigment epithelium-derived factor (PEDF), a potent endogenous anti-angiogenic molecule, is significantly increased in sepsis, but its role in endothelial dysfunction has not been defined. To assess the role of PEDF in the vasculature, we evaluated the effects of exogenous PEDF in vivo using a mouse model of cecal ligation and puncture (CLP)-induced sepsis and in vitro using human dermal microvascular endothelial cells (HDMECs). In addition, PEDF was inhibited using a PEDF-monoclonal antibody (PEDF-mAb) or recombinant lentivirus vectors targeting PEDF receptors, including adipose triglyceride lipase (ATGL) and laminin receptor (LR). Our results showed that exogenous PEDF induced vascular hyperpermeability, as measured by extravasation of Evans Blue (EB), dextran and microspheres in the skin, blood, trachea and cremaster muscle, both ...
Binding properties of the native Thermomyces lanuginosa lipase (Tll), the inactive mutant of Tll (S146A; active Ser146 mutated to Ala), and the non-glycosylated mutant of Tll (N33Q) were determined using fluorescence spectroscopy. Tll, S146A mutant and N33Q mutant show significant different binding behavior to phosphatidylcholine (PC) and phosphatidylglycerol (PG) liposomes. Generally, weaker association of lipase molecules is observed to PC liposomes than to PG liposomes. Strong lipase-lipid interactions are observed for the S146A mutant, which is less pronounced for Tll and the N33Q variant. Addition of fatty acid to PG liposomes reduces significantly the binding affinity of the lipases. This effect is less pronounced in fatty acid/PC liposomes. Although the catalytic activity of the N33Q mutant is comparable to Tll, the non-glycosylated variant shows generally lower binding affinity to PC or PG matrix than Tll. Addition of the substrate analog benzene boronic acid (BBA) increases the binding ...
In comparison to the adult birds, young chickens and turkeys have a reduced ability to use dietary fat. It was of interest to investigate the role of lipase in fat malabsorption in young birds. It was hypothesized that fat malabsorption in young chickens and turkeys is due to an insufficiency of pancreatic lipase. It was further hypothesized that fat utilization in young birds can be improved by the use of dietary lipase sources. The first in vitro experiment characterized the activity and stability of mammalian, fungal and bacterial lipase sources when exposed to conditions associated with the proventriculus of young birds. The results of this study demonstrated that bacterial Pseudomonas sp. and Chromobacterium viscosum lipase sources are more stable under conditions that mimic the glandular stomach of young birds. Aspergillus niger lipase also showed a relatively high activity in acidic conditions. Mammalian crude porcine lipase was irreversibly inhibited in these conditions. The second in ...
TY - JOUR. T1 - Enzymatic resolution of (±)-cis-2-aminocyclopentanol and (±)-cis-2- aminocyclohexanol. AU - Luna, Amparo. AU - Astorga, Covadonga. AU - Fülöp, F.. AU - Gotor, Vicente. PY - 1998/12/24. Y1 - 1998/12/24. N2 - (±)-cis-N-Benzyloxycarbonyl-2-aminocyclopentanol was efficiently resolved by O-acylation with Pseudomonas cepacia lipase, as was (±)-cis-N- benzyloxycarbonyl-2-aminocyclohexanol when Candida antarctica lipase was used.. AB - (±)-cis-N-Benzyloxycarbonyl-2-aminocyclopentanol was efficiently resolved by O-acylation with Pseudomonas cepacia lipase, as was (±)-cis-N- benzyloxycarbonyl-2-aminocyclohexanol when Candida antarctica lipase was used.. UR - http://www.scopus.com/inward/record.url?scp=0032564662&partnerID=8YFLogxK. UR - http://www.scopus.com/inward/citedby.url?scp=0032564662&partnerID=8YFLogxK. U2 - 10.1016/S0957-4166(98)00482-0. DO - 10.1016/S0957-4166(98)00482-0. M3 - Article. AN - SCOPUS:0032564662. VL - 9. SP - 4483. EP - 4487. JO - Tetrahedron Asymmetry. JF - ...
Experiments were conducted to study the effects of high density lipoprotein (HDL) and apolipoproteins C, E, and A on lipoprotein lipase activity in rhesus monkeys. The lipoprotein lipase activity was inhibited up to 32 +/- 6 per cent by monkey HDL. This inhibition was considerably decreased (2 +/- 0.02%) by using apolipoprotein-poor HDL. Apolipoproteins C and E inhibited the hydrolysis of activated intralipid by monkey lipoprotein lipase to a maximum of 83 +/- 7 and 57 +/- 5 per cent respectively. Apolipoprotein A produced little inhibition of lipoprotein lipase activity. The results of these studies demonstrate that HDL and apolipoproteins compete with the substrate for the binding to lipoprotein lipase in rhesus monkeys.
in Fungal Genetics and Biology (2005), 42(3), 264-274. In the lipolytic yeast Yarrowia lipolytica, the LIP2 gene was previously reported to encode all extracellular lipase. The growth of a Deltalip2 strain on triglycerides as sole carbon source suggest all ... [more ▼]. In the lipolytic yeast Yarrowia lipolytica, the LIP2 gene was previously reported to encode all extracellular lipase. The growth of a Deltalip2 strain on triglycerides as sole carbon source suggest all alternative pathway for triglycerides utilisation ill this yeast. Here, we describe the isolation and the characterisation of the LIP7 and LIP8 genes which were found to encode a 366 and a 371-amino acid precursor protein, respectively. These proteins which belong to the triacylglycerol hydrolase family (EC 3.1.1.3) presented a high homology with the extracellular lipase CdLIP2 and CdLIP3 from Candida deformans. The physiological function of the lipase isoenzymes was investigated by creating single and multi-disrupted strains. ...
A lipase gene (atl) was cloned from Aspergillustamarii FS132 for the first time. The gene was found to have an open reading frame of 1024 base pairs (bp), and the coding region of the gene contained two introns (51 bp and 52 bp). Multi-alignment analysis of the deduced amino acid sequence indicated high homology between the enzyme and mono- and diacylglycerol lipases from fungi Aspergillus. The recombinant lipase was expressed in Pichia pastoris GS115 cells. The recombinant lipase was found to have a molecular mass of 36.7 kDa, and it exhibited lipase activity of 20 U/mL in culture supernatant when tributyrin was used as the substrate.
Sixteen pigs from 2 distinct genetic lines (LGAH and VFIL) obtained after eight generations of divergent selection for high (H) and low (L) lean tissue growth rate with ad-libitum feeding (LGA) and voluntary feed intake (VFI), respectively, were used in this study. The objectives of this investigation were to establish appropriate working conditions for the postheparin plasma lipoprotein lipase (LPL) assay and to study relationships between fat deposition and plasma lipids, very low density lipoprotein (VLDL) lipids, VLDL-subfractions and postheparin plasma LPL activity in growing pigs. Four preliminary experiments were performed to determine the appropriate working conditions for the postheparin plasma LPL assays. Postheparin plasma preincubated with SDS (20-50 mM) at 26 C for 45 minutes inhibited hepatic lipase activity. A total of 2 l VLDL/assay produced maximum stimulation of LPL activity. Postheparin plasma protein and increasing incubation time contributed an optimum response. LGAH pigs ...
article{5a0b5a06-4e09-4a23-a38a-02712684b3d8, abstract = {The location of lipoprotein lipase activity in rat adipose tissue was studied using intact epididymal fat pads, isolated adipocytes, and lipoprotein lipase activity secreted from adipocytes as enzyme sources. The enzyme activities of these preparations were characterized by gel filtration. The method used for isolation of adipocytes had been modified to minimize activation of lipoprotein lipase during the procedures. Extracts of intact adipose tissue separated into two major lipoprotein lipase activity peaks, designated a and b, the a fraction representing about 30 (fasted rats) to 50% (fed rats) of the total enzyme activity. An intermediate fraction (designated i) was frequently observed. Extracts of isolated adipocytes from fed rats contained about 35% and those from fasted rats about 65% of the lipoprotein lipase activity present in intact tissue. The b fraction constituted 80--97% of the adipocyte lipoprotein lipase ...
The goal of this thesis is to synthesize enantiopure (R)-1-((1H-indol-4-yl)oxy)-3-chloropropan-2-ol ((R)-2) and synthesize (S)-pindolol ((S)-5) from it.A chemoenzymatic synthesis of theβ-blocker (S)-pindolol ((S)-5) was performed from 1H-indol-4-ol (1). This synthesis was performed by first doing an organic synthesis to synthesise 1-((1H-indol-4-yl)oxy)-3-chloropropan-2-ol (2) from1H-indol-4-ol (1). This gave a 76 % yield of pure 2 over two reaction steps after purification by flash column. The enzyme Candida antarctica Lipase B (CALB) was used as a stereoselective catalyst to produce (R)-1-((1H-indol-4-yl)oxy)-3-chloropropan-2-ol ((R)-2) and (S)-1-((1H-indol-4-yl)oxy)-3-chloropropan-2-yl butyrate ((S)-4) from the racemic mixture of 2. The last step was to synthesize (S)-pindolol ((S)-5)from (R)-1-((1H-indol-4-yl)oxy)-3-chloropropan-2-ol ((R)-2). The enzyme reaction was performed by reacting 1-((1H-indol-4-yl)oxy)-3-chloropropan-2-ol (2) with vinyl butyrate using the enzyme CALB as a catalyst ...
The purpose of this Application is to seek approval to permit the use of the enzyme Triacylglycerol lipase from Trichoderma reesei as a processing aid in the manufacturing of cereal-based products.. Approval Report - 21 March 2019 (pdf 887 kb) , (word 144 kb). ...
Supplements of a highly purified lipase were given with fat test meals to human subjects and dogs in order to determine the effect on blood lipid levels. The optical density and hence lipid levels of the blood plasmas were lowered in all subjects when sufficient lipase was ingested. The total esterified fatty acid and triglyceride determinations confirmed this measurement of the decrease acid and triglyceride determinations confirmed this measurement of the decrease in blood lipid levels. Human subjects with lowered fasting O.D. values and E.F.A. appeared to require more lipase to obtain this effect. The blood cholesterol values of normal subjects were not affected, nor was that of a hyperlipemic subject who ingested the lipase for over a four week test period. In all human subjects, the serum lipase values were elevated when the blood lipid levels were lowered. The association of elevated blood lipase levels with decreased blood lipids suggest the possibility of a lipolytic action in the
Endothelial lipase (EL) is a recently discovered member of the lipoprotein lipase gene family that hydrolyzes HDL phospholipids ex vivo and reduces HDL cholesterol (HDL-C) levels when overexpressed in vivo in mice. To gain further insight into the physiological role of EL in the metabolism of HDL in vivo, studies were performed in which EL was inhibited in wild-type, hepatic lipase knockout (HL-/-), and human apoA-I transgenic mice by intravenous infusion of a polyclonal antibody inhibitory to murine EL. As compared with infusion of a control antibody, infusion of the inhibitory antibody resulted in a 25-60% increase in HDL-C levels in the three mouse models, with the peak HDL-C levels occurring at 48 hours after injection. Inhibition of EL also generated larger HDL particles in the HL-/- mice. The clearance of HDL phospholipid was significantly slower in human apoA-I transgenic mice injected with an antibody against murine EL (mEL) than in mice injected with a control antibody. We conclude that ...
Immobilization of lipases is gammg importance due to a broad variety of industrial applications they catalyze. In this study, lipase from Burkholderia cepacia was first cross linked with glutaraldehyde followed by entrapment into hybrid matrix of alginate and K -carrageenan polymers. The effect of various parameters like pH, temperature, reusability, enzyme leakage, solvent and storage stability on immobilized lipase were studied. A higher activity yield of 89.26% was observed after immobilization. The immobilized lipase_ also retained 84.02% of its initial activity following two weeks of storage in T/Ca (Tris-CaCh)buffer at 4 ° C. Comparative kinetic parameters Km and Vmax values were found to be 0.39 µM and 10 µmol/min for free lipase and 0.45 µM and 9.09 µmol/min for immobilized lipase respectively. A significant enzyme leakage reduction of 65. 76% was observed as compared to the enzyme immobilized in hybrid matrix without crosslinking. The immobilized lipase also gave better results for ...
Using enrichment procedures, 45 organic solvent-tolerant lipase producer bacterial strains were screened from areas contaminated by oil and organic solvents. Among the strains, 15 isolates exhibited extreme stability toward organic solvents and high lipolytic activity. The NEB-1 isolate which was later identified as Pseudomonas sp. strain NEB-1 by biochemical tests and 16S rDNA gene sequence analysis was selected based on extremely high tolerance to organic solvents and maximum lipase production. Biochemical studies revealed that the crude lipase was stable at temperatures between 20 ºC and 60 ºC and pH ranges of 4 to 11 for 1 h. Optimum pH and temperature of the enzyme were revealed to be 9.5 and 70 ºC, respectively. The crude lipase showed remarkable tolerance in presence of different organic solvents with a broad range of hydrophobicity characteristics. The solvent stable lipase showed an attractive potency for application in biocatalysis in non-aqueous systems and biodiesel
One application that takes advantage of the hydrolytic ability of lipase is the production of food-flavoring agents. This application relies on the fact that the fatty acid released from triglyceride upon hydrolysis by lipase gives different flavors depending on the type of fatty acid being released. For example, among the fatty acids obtained by hydrolyzing cows milk triglycerides with lipases, short-chain fatty acids give off a cheesy aroma, those fatty acids with longer chain give off a milky smell, and those with even longer chain give off a buttery scent. Thus, lipases are used widely as flavor-intensifying food additive in various food products, such as dairy products, confectioneries, ice cream and industrial-grade cheese. Lipases are also used to remove lipids in food products. For example, lipids from yolk that are mixed in with the egg white can be removed by breaking the lipids down with lipases ...
pancreatic lipase related protein 2: from human (hPLRP2) & guinea pig (gPLRP2); highly homologous to human pancreatic lipase (hPL), but its lipolytic activity is profoundly different from hPL; amino acid sequence has been determined
Abstract: Many proteins are synthesized as precursors, with propeptides playing a variety of roles such as assisting in folding or preventing them from being active within the cell. While the precise role of the propeptide in fungal lipases is not completely understood, it was previously reported that mutations in the propeptide region of the Rhizomucor miehei lipase have an influence on the activity of the mature enzyme, stressing the importance of the amino acid composition of this region. We here report two structures of this enzyme in complex with its propeptide, which suggests that the latter plays a role in the correct maturation of the enzyme. Most importantly, we demonstrate that the propeptide shows inhibition of lipase activity in standard lipase assays and propose that an important role of the propeptide is to ensure that the enzyme is not active during its expression pathway in the original host ...
A plate assay to detect bacterial lipase (EC 3.1.1.3) in a medium containing trioleoylglycerol and the fluorescent dye rhodamine B is presented. Substrate hydrolysis causes the formation of orange fluorescent halos around bacterial colonies visible upon UV irradiation. The logarithm of lipase activity from cell-free culture supernatants is linearly correlated with the diameter of halos, thereby allowing quantitation of lipase activities ranging from 1 to 30 nkat. ...
Microorganisms are the most proficient decomposers in nature, using secreted enzymes in the hydrolysis of lignocellulose. As such, they present the most abundant source for discovery of new enzymes. Acremonium alcalophilum is the only known cellulolytic fungus that thrives in alkaline conditions and can be cultured readily in the laboratory. Its optimal conditions for growth are 30°C and pH 9.0-9.2. The genome sequence of Acremonium alcalophilum has revealed a large number of genes encoding biomass-degrading enzymes. Among these enzymes, lipases are interesting because of several industrial applications including biofuels, detergent, food processing and textile industries. We identified a lipA gene in the genome sequence of Acremonium alcalophilum, encoding a protein with a predicted lipase domain with weak sequence identity to characterized enzymes. Unusually, the predicted lipase displays ≈ 30% amino acid sequence identity to both feruloyl esterase and lipase of Aspergillus niger. LipA, when
An automated colorimetric method for determining lipase activity in canine sera was evaluated for precision, linearity and correlation to existing assay methods. The colorimetric method was a commercial reagent that used a series of enzymatic reactions based on the hydrolysis of 1,2 diglyceride by pancreatic lipase. Within-run and between-run coefficients of variation were 7 y) dogs using this assay. It was concluded that the automated colorimetric assay was a reliable indicator of canine serum Show moreAn automated colorimetric method for determining lipase activity in canine sera was evaluated for precision, linearity and correlation to existing assay methods. The colorimetric method was a commercial reagent that used a series of enzymatic reactions based on the hydrolysis of 1,2 diglyceride by pancreatic lipase. Within-run and between-run coefficients of variation were 7 y) dogs using this assay. It was concluded that the automated colorimetric assay was a reliable indicator of canine serum ...
A thermostable extracellular lipase of Geobacillus sp. strain T1 was cloned in a prokaryotic system. Sequence analysis revealed an open reading frame of 1,251 bp in length which codes for a polypeptide of 416 amino acid residues. The polypeptide was composed of a signal peptide (28 amino acids) and a mature protein of 388 amino acids. Instead of Gly, Ala was substituted as the first residue of the conserved pentapeptide Gly-X-Ser-X-Gly. Successful gene expression was obtained with pBAD, pRSET, pET, and pGEX as under the control of araBAD, T7, T7 lac, and tac promoters, respectively. Among them, pGEX had a specific activity of 30.19 Umg−1 which corresponds to 2927.15 Ug−1 of wet cells after optimization. The recombinant lipase had an optimum temperature and pH of 65°C and pH 9, respectively. It was stable up to 65°C at pH 7 and active over a wide pH range (pH 6-11). This study presents a rapid cloning and overexpression, aimed at improving the enzyme yield for successful industrial ...
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TY - JOUR. T1 - Effects of plasma adrenaline on hormone-sensitive lipase at rest and during moderate exercise in human skeletal muscle. AU - Watt, Matthew James. AU - Stellingwerff, Trent. AU - Heigenhauser, George J F. AU - Spriet, Lawrence L. PY - 2003. Y1 - 2003. M3 - Article. VL - 550. SP - 325. EP - 332. JO - The Journal of Physiology. JF - The Journal of Physiology. SN - 0022-3751. IS - Pt. 1. ER - ...
Metabolism is a highly integrated process that is coordinately regulated between tissues and within individual cells. FoxO proteins are major targets of insulin action and contribute to the regulation of gluconeogenesis, glycolysis, and lipogenesis in the liver. However, the mechanisms by which FoxO proteins exert these diverse effects in an integrated fashion remain poorly understood. We report that FoxO proteins also exert important effects on intrahepatic lipolysis and fatty acid oxidation via the regulation of adipose triacylglycerol lipase (ATGL), which mediates the first step in lipolysis, and its inhibitor, the G0/S1 switch 2 gene (G0S2). We also find that ATGL-dependent lipolysis plays a critical role in mediating diverse effects of FoxO proteins in the liver, including effects on gluconeogenic, glycolytic, and lipogenic gene expression and metabolism. These results indicate that intrahepatic lipolysis plays a critical role in mediating and integrating the regulation of glucose and lipid ...
TY - JOUR. T1 - Tgl4p and Tgl5p, two triacylglycerol lipases of the yeast Saccharomyces cerevisiae are localized to lipid particles. AU - Athenstaedt, Karin. AU - Daum, Günther. PY - 2005. Y1 - 2005. M3 - Article. VL - 280. SP - 37301. EP - 37109. JO - The Journal of Biological Chemistry. JF - The Journal of Biological Chemistry. SN - 0021-9258. ER - ...
Lipoprotein lipase is the principal enzyme that hydrolyzes circulating triglycerides and liberates free fatty acids that can be used as energy by cardiac muscle. Although lipoprotein lipase is expressed by and is found on the surface of cardiomyocytes, its transfer to the luminal surface of endothelial cells is thought to be required for lipoprotein lipase actions. To study whether nontransferable lipoprotein lipase has physiological actions, we placed an α-myosin heavy-chain promoter upstream of a human lipoprotein lipase minigene construct with a glycosylphosphatidylinositol anchoring sequence on the carboxyl terminal region. Hearts of transgenic mice expressed the altered lipoprotein lipase, and the protein localized to the surface of cardiomyocytes. Hearts, but not postheparin plasma, of these mice contained human lipoprotein lipase activity. More lipid accumulated in hearts expressing the transgene; the myocytes were enlarged and exhibited abnormal architecture. Hearts of transgenic mice ...
PubMed journal article: Effect of fenofibrate on plasma lipoprotein composition and kinetics in patients with complete hepatic lipase deficiency. Download Prime PubMed App to iPhone, iPad, or Android
Lipases are one of the most valuable classes of enzymes of high economic importance. Bacterial lipases vary widely in enzymatic properties and substrate specificities. Consequently, they are currently receiving much attention because of their potential applications in various industrial processes and biotechnological applications as in fat, food ingredients, detergents, surfactants, textile industries and oil processing. Microbial lipases have wide application in the processing of leather, domestic, industrial wastes and pharmaceutical industries. The need for thermostable lipase enzymes is steadily rising and the isolation of lipases from thermostable microorganisms is highly requisite. In a screening program for isolation of thermophilic lipase-producing bacteria, a number of thermophilic bacteria were isolated from Al- Hassa region, Saudi Arabia. Among 93 isolates, potent bacterial candidates were identified based on biochemical characteristics, RAPD-PCR, and 16S rRNA gene sequencing. ...