Amylases
alpha-Amylases
Saliva
Pancreas
Parotid Gland
Inhibition of plant-pathogenic fungi by a corn trypsin inhibitor overexpressed in Escherichia coli. (1/1178)
The cDNA of a 14-kDa trypsin inhibitor (TI) from corn was subcloned into an Escherichia coli overexpression vector. The overexpressed TI was purified based on its insolubility in urea and then refolded into the active form in vitro. This recombinant TI inhibited both conidium germination and hyphal growth of all nine plant pathogenic fungi studied, including Aspergillus flavus, Aspergillus parasiticus, and Fusarium moniliforme. The calculated 50% inhibitory concentration of TI for conidium germination ranged from 70 to more than 300 microgram/ml, and that for fungal growth ranged from 33 to 124 microgram/ml depending on the fungal species. It also inhibited A. flavus and F. moniliforme simultaneously when they were tested together. The results suggest that the corn 14-kDa TI may function in host resistance against a variety of fungal pathogens of crops. (+info)Insertion analysis of putative functional elements in the promoter region of the Aspergillus oryzae Taka-amylase A gene (amyB) using a heterologous Aspergillus nidulans amdS-lacZ fusion gene system. (2/1178)
Expression of the Taka-amylase A gene (amyB) of Aspergillus oryzae is induced by starch or maltose. The A. oryzae amyB gene promoter contains three highly conserved sequences, designated Regions I, II, and III, compared with promoter regions of the A. oryzae glaA encoding glucoamylase and the agdA encoding alpha-glucosidase. To identify the function of these sequences within the amyB promoter, various fragments containing conserved sequences in the amyB promoter were introduced into the upstream region of the heterologous A. nidulans amdS gene (encoding acetamidase) fused to the Escherichia coli lacZ gene as a reporter. Introduction of the sequence between -290 to -233 (the number indicates the distance in base pairs from the translation initiation point (+1)) containing Region III significantly increased the expression of the lacZ reporter gene in the presence of maltose. The sequence between -377 to -290 containing Region I also increased the lacZ activity, but its maltose inducibility was less than that of Region III. The sequence between -233 to -181 containing Region II had no effect on the expression. These results indicated that Region III is most likely involved in the maltose induction of the amyB gene expression. (+info)Overexpression of BiP in tobacco alleviates endoplasmic reticulum stress. (3/1178)
To study the role of the lumenal binding protein (BiP) in the transport and secretion of proteins, we have produced plants with altered BiP levels. Transgenic plants overexpressing BiP showed dramatically increased BiP mRNA levels but only a modest increase in BiP protein levels. The presence of degradation products in BiP overproducers suggests a regulatory mechanism that increases protein turnover when BiP is abundant. Antisense inhibition of BiP synthesis was not successful, demonstrating that even a minor reduction in the basal BiP level is deleterious to cell viability. Overexpression of BiP leads to downregulation of the basal transcript levels of endogenous BiP genes and greatly reduces the unfolded protein response. The data confirm that BiP transcription is regulated via a feedback mechanism that involves monitoring of BiP protein levels. To test BiP activity in vivo, we designed a functional assay, using the secretory protein alpha-amylase and a cytosolic enzyme as a control for cell viability. During tunicamycin treatment, an overall reduction of alpha-amylase synthesis was observed when compared with the cytosolic marker. We show that the tunicamycin effect is due to the depletion of BiP in the endoplasmic reticulum because coexpressed BiP alone is able to restore efficient alpha-amylase synthesis. This is a novel assay to monitor BiP activity in promoting secretory protein synthesis in vivo. (+info)Differential dependence of levansucrase and alpha-amylase secretion on SecA (Div) during the exponential phase of growth of Bacillus subtilis. (4/1178)
SecA, the translocation ATPase of the preprotein translocase, accounts for 0.25% of the total protein in a degU32(Hy) Bacillus subtilis strain in logarithmic phase. The SecA level remained constant irrespective of the demand for exoprotein production but dropped about 12-fold during the late stationary phase. Modulation of the level of functional SecA during the exponential phase of growth affected differently the secretion of levansucrase and alpha-amylase overexpressed under the control of the sacB leader region. The level of SecA was reduced in the presence of sodium azide and in the div341 thermosensitive mutant at nonpermissive temperatures. Overproduction of SecA was obtained with a multicopy plasmid bearing secA. The gradual decrease of the SecA level reduced the yield of secreted levansucrase with a concomitant accumulation of unprocessed precursor in the cells, while an increase in the SecA level resulted in an elevation of the production of exocellular levansucrase. In contrast, alpha-amylase secretion was almost unaffected by high concentrations of sodium azide or by very low levels of SecA. Secretion defects were apparent only under conditions of strong SecA deprivation of the cell. These data demonstrate that the alpha-amylase and levansucrase precursors markedly differ in their dependency on SecA for secretion. It is suggested that these precursors differ in their binding affinities for SecA. (+info)Genetic regulation of tissue-specific expression of amylase structural genes in Drosophila melanogaster. (5/1178)
Laboratory strains of Drosophila melanogaster were screened for spatial variations in adult midgut alpha-amylase (1,4-alpha-D-glucan glucanohydrolase, EC 3.2.1.1) expression. No strain-specific differences were found anteriorly, but three patterns of activity were discerned in the posterior midgut: A, activity throughout most of the region; B, activity in the anterior part of the region; and C, little or no activity. Alleles of a control gene, map, are responsible for this tissue-specific regulation of activity; e.g., mapA homozygotes produce the A pattern and mapC homozygotes the C pattern. The map locus was placed at 2--80 +/- on the genetic map of chromosome 2R, about two crossover units distal to the Amy structural gene region for alpha-amylase. Electrophoretic studies showed that mapA is trans acting in mapA/mapC flies, allowing expression of amylase isozymes coded for by genes on the opposite chromosome. The map gene behaves as a temporal gene that is clearly separable from the tightly linked, duplicated Amy structural genes. (+info)Molecular cloning and primary structure analysis of porcine pancreatic alpha-amylase. (6/1178)
A cDNA library was constructed in a Uni-ZAP XR vector using mRNA isolated from porcine pancreas. A full-length alpha-amylase cDNA was obtained using a combination of library screening and nested polymerase chain reaction. Sequencing of the clone revealed a 1536-nucleotide (nt) open reading frame encoding a protein of 496 amino acid (aa) residues with a signal peptide of 15 aa. The calculated molecular mass of the enzyme was 55354 Da, in accordance with those of the purified porcine pancreatic alpha-amylase forms (PPAI and PPAII) as determined by mass spectrometry. A comparison of the deduced aa sequence with published peptidic sequences of PPAI identified a number of mismatches. The sequence of the cDNA reported here provides a sequence reference for PPA in excellent agreement with the refined three-dimensional structures of both PPAI and PPAII. No evidence for a second variant was found in the cDNA library and it is most likely that PPAI and PPAII are two forms of the same protein. The primary structure of PPA shows high homology with human, mouse and rat pancreatic alpha-amylases. The 304-310 region, corresponding to a mobile loop involved in substrate binding and processing near the active site, is fully conserved. (+info)Cloning, mutagenesis, and structural analysis of human pancreatic alpha-amylase expressed in Pichia pastoris. (7/1178)
Human pancreatic alpha-amylase (HPA) was expressed in the methylotrophic yeast Pichia pastoris and two mutants (D197A and D197N) of a completely conserved active site carboxylic acid were generated. All recombinant proteins were shown by electrospray ionization mass spectrometry (ESI-MS) to be glycosylated and the site of attachment was shown to be Asn461 by peptide mapping in conjunction with ESI-MS. Treatment of these proteins with endoglycosidase F demonstrated that they contained a single N-linked oligosaccharide and yielded a protein product with a single N-acetyl glucosamine (GlcNAc), which could be crystallized. Solution of the crystal structure to a resolution of 2.0 A confirmed the location of the glycosyl group as Asn461 and showed that the recombinant protein had essentially the same conformation as the native enzyme. The kinetic parameters of the glycosylated and deglycosylated wild-type proteins were the same while the k(cat)/Km values for D197A and D197N were 10(6)-10(7) times lower than the wild-type enzyme. The decreased k(cat)/Km values for the mutants confirm that D197 plays a crucial role in the hydrolytic activity of HPA, presumably as the catalytic nucleophile. (+info)Chemical modification of lysine side chains of cyclodextrin glycosyltransferase from Thermoanaerobacter causes a shift from cyclodextrin glycosyltransferase to alpha-amylase specificity. (8/1178)
Cyclodextrin glycosyltransferases and alpha-amylases are two groups of enzymes with related secondary structures. However, cyclodextrin glycosyltransferases display transferase activities not present in alpha-amylases, probably derived from the existence of two more domains and different amino acid sequences. The hydrolytic activity of cyclodextrin glycosyltransferases is generally quite low, except for two cyclodextrin glycosyltransferases from termophiles. In this work, we have carried out the chemical modification (with acetic anhydride) of the amino groups of cyclodextrin glycosyltransferase from Thermoanaerobacter to assess their contributions to protein function. The acetylated cyclodextrin glycosyltransferase showed a significant reduction of its cyclization, coupling and disproportionation activities. Surprisingly, the hydrolytic (saccharifying) activity was slightly enhanced. These results suggest the participation of one or more lysine side chains in the interactions contributing to the transferase activity, either in any of the S11 subsites or in the acceptor binding site. (+info)Salivary alpha-amylases are a type of enzyme that are secreted by the salivary glands in humans and other mammals. These enzymes play a crucial role in the digestion of carbohydrates, specifically starches and glycogen, by breaking down these complex molecules into simpler sugars such as maltose, isomaltose, and maltotriose.
Salivary alpha-amylases are part of a larger family of enzymes known as alpha-amylases, which also include pancreatic alpha-amylases that are secreted by the pancreas and play a similar role in digestion. However, salivary alpha-amylases have some unique properties, such as being more resistant to denaturation by heat and acid than pancreatic alpha-amylases.
Salivary alpha-amylases are also used as a biomarker in forensic science for the identification of individuals, as they exhibit variations in their protein structure that can be used to distinguish between different people. Additionally, changes in salivary alpha-amylase levels have been associated with various physiological and psychological states, such as stress, anxiety, and arousal.
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.
Alpha-amylases are a type of enzyme that breaks down complex carbohydrates, such as starch and glycogen, into simpler sugars like maltose, maltotriose, and glucose. These enzymes catalyze the hydrolysis of alpha-1,4 glycosidic bonds in these complex carbohydrates, making them more easily digestible.
Alpha-amylases are produced by various organisms, including humans, animals, plants, and microorganisms such as bacteria and fungi. In humans, alpha-amylases are primarily produced by the salivary glands and pancreas, and they play an essential role in the digestion of dietary carbohydrates.
Deficiency or malfunction of alpha-amylases can lead to various medical conditions, such as diabetes, kidney disease, and genetic disorders like congenital sucrase-isomaltase deficiency. On the other hand, excessive production of alpha-amylases can contribute to dental caries and other oral health issues.
Sialorrhea is the medical term for excessive drooling or saliva production. It's not necessarily a condition where the person produces too much saliva, but rather, they are unable to control the normal amount of saliva in their mouth due to various reasons such as neurological disorders, developmental disabilities, or structural issues that affect swallowing and oral motor function.
Common causes include cerebral palsy, Parkinson's disease, amyotrophic lateral sclerosis (ALS), Down syndrome, stroke, intellectual disability, and certain medications. Treatment options vary depending on the cause and severity of the condition and may include medication adjustments, behavioral interventions, oral devices, or even surgical procedures in severe cases.
Saliva is a complex mixture of primarily water, but also electrolytes, enzymes, antibacterial compounds, and various other substances. It is produced by the salivary glands located in the mouth. Saliva plays an essential role in maintaining oral health by moistening the mouth, helping to digest food, and protecting the teeth from decay by neutralizing acids produced by bacteria.
The medical definition of saliva can be stated as:
"A clear, watery, slightly alkaline fluid secreted by the salivary glands, consisting mainly of water, with small amounts of electrolytes, enzymes (such as amylase), mucus, and antibacterial compounds. Saliva aids in digestion, lubrication of oral tissues, and provides an oral barrier against microorganisms."
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.
The parotid gland is the largest of the major salivary glands. It is a bilobed, accessory digestive organ that secretes serous saliva into the mouth via the parotid duct (Stensen's duct), located near the upper second molar tooth. The parotid gland is primarily responsible for moistening and lubricating food to aid in swallowing and digestion.
Anatomically, the parotid gland is located in the preauricular region, extending from the zygomatic arch superiorly to the angle of the mandible inferiorly, and from the masseter muscle anteriorly to the sternocleidomastoid muscle posteriorly. It is enclosed within a fascial capsule and has a rich blood supply from the external carotid artery and a complex innervation pattern involving both parasympathetic and sympathetic fibers.
Parotid gland disorders can include salivary gland stones (sialolithiasis), infections, inflammatory conditions, benign or malignant tumors, and autoimmune diseases such as Sjögren's syndrome.
Alpha 1-antitrypsin (AAT, or α1-antiproteinase, A1AP) is a protein that is primarily produced by the liver and released into the bloodstream. It belongs to a group of proteins called serine protease inhibitors, which help regulate inflammation and protect tissues from damage caused by enzymes involved in the immune response.
Alpha 1-antitrypsin is particularly important for protecting the lungs from damage caused by neutrophil elastase, an enzyme released by white blood cells called neutrophils during inflammation. In the lungs, AAT binds to and inhibits neutrophil elastase, preventing it from degrading the extracellular matrix and damaging lung tissue.
Deficiency in alpha 1-antitrypsin can lead to chronic obstructive pulmonary disease (COPD) and liver disease. The most common cause of AAT deficiency is a genetic mutation that results in abnormal folding and accumulation of the protein within liver cells, leading to reduced levels of functional AAT in the bloodstream. This condition is called alpha 1-antitrypsin deficiency (AATD) and can be inherited in an autosomal codominant manner. Individuals with severe AATD may require augmentation therapy with intravenous infusions of purified human AAT to help prevent lung damage.
Alpha amylase inhibitor
Α-Amylase
Oligosaccharide 4-alpha-D-glucosyltransferase
Amylase
Β-Amylase
Plant defensin
Glucan 1,4-alpha-maltohydrolase
AMY1C
Streptomyces corchorusii
Dental plaque
Exoenzyme
AMY2B
Maltase
Icodextrin
Glycogen debranching enzyme
AMY1A
AMY2A
Acarbose
Raymond L. Rodriguez
3,5-Dinitrosalicylic acid
Polysaccharide
Streptomyces tendae
Sprout damage
Glucansucrase
Streptomyces griseosporeus
Bacillus amyloliquefaciens
Parotid gland
Isomaltase
Glycogen branching enzyme
Defensin
Alpha amylase inhibitor - Wikipedia
1QHP: FIVE-DOMAIN ALPHA-AMYLASE FROM BACILLUS STEAROTHERMOPHILUS, MALTOSE COMPLEX
Assessment of Antioxidative and Alpha-Amylase Potential of Polyherbal Extract
Alpha-Amylase, Granules, 100 g | Carolina Biological Supply
alpha-amylase Archives - Ideas Galore
Properties of the Alpha Amylase from Moringa oleifera Seeds
Hypothesis that alpha-amylase evokes regulatory mechanisms originating in the pancreas, gut and circulation, which govern...
Behavior problems in youth may show a higher salivary cortisol - alpha amylase coordination - Salimetrics
Alpha Amylase Activity in Liquid Egg | Lovibond
Alpha-glucosidase and alpha-amylase inhibiting thiodiketopiperazines from the endophytic fungus Setosphaeria rostrata isolated...
Alpha-Amylase HR Reagent - Analysis of alpha-amylase | Megazyme
Alpha Amylase Enzyme
Wheat Alpha Amylase
Alpha Amylase - UPC Food Search
Clinical Chemistry Human Alpha-Amylase Liquicolor
Alpha Amylase / Fungal Diastase</span>
Food Production Alpha Amylase Enzyme - Joinedfortunechemical
Still Spirits Distiller's Alpha-Amylase Enzyme
Alpha-Amylase Enzyme - Grape Grain And Bean
Fungal Alpha-Amylase FAA-280-Boli Bioproducts
Alpha-Amylase Enzyme 12g | Spokane Brewing Supp
Alpha-amylase HTA-430 (Thermostable)-Boli Bioproducts
Human Alpha-amylase 2B , AMY2B ELISA Kit
SciELO - Brazil - Culture conditions for the production of thermostable amylase by Bacillus sp Culture conditions for the...
Alpha amylase-O00A-Wuxi Biortus Biosciences Co. Ltd.
Alpha Amylase Enzyme 1.5oz - The Homebrew Exchange
Correlating Molecular Interactions with Solubility of Alpha-Amylase from Bacillus Licheniformis<...
alpha-Amylase from Bacillus sp. | Merck Life Science Indonesia
Liquid Desizing Textile Alpha Amylase Enzyme With Low Dosage Rate
Extracellular thermostable alpha-amylase from Bacillus stearothermophilus Q8<...
Starch21
- Crude alpha amylase preparation from Moringa oleifera seeds was used to hydrolyze starch. (scialert.net)
- Site directed mutagenesis of histidine 93, aspartic acid 180, glutamic acid 205, histidine 290 and aspartic acid291 at the active site and tryptophan 279 at the raw starch binding site in barley α-amylase. (scialert.net)
- Fungal Diastase (fungal alpha amylase) has both liquefying and saccharifying actions on starch, liberating a mixture of glucose and maltose as digestion products. (meteoricbiopharma.com)
- Alpha-Amylase is a bacterial-derived enzyme that breaks down starch into dextrins and simple sugars during mashing. (brewsrq.com)
- Please note that some starch substrates, such as corn starch, may require longer boiling times in order to fully break down and gelatinize the starch prior to the application of the Alpha-amylase enzyme. (brewsrq.com)
- Thermostable powdered alpha-amylase enzyme for hydrolysis of long-chain starch molecules into short-chain dextrins. (grapegrainandbean.com)
- In the production of malt syrup, first use heat-stable alpha-amylase for starch liquefaction so that DE value of the liquefied solution reaches 13∼20%, then cool down to 55∼ 58°C, adjust pH to 5.0 ∼ 5.5. (bolibio.com)
- HTA-430 is a low pH tolerated Heat-stable Alpha-Amylase widely used in the production of starch sugar. (bolibio.com)
- It is a liquid endoamylase that can rapidly decrease the viscosity of gelatinous starch solutions by randomly hydrolyzing starch, glycogen and its degradation products within the alpha-1,4 glucosidic bonds to produce soluble dextrins and oligosaccharides. (bolibio.com)
- As a robust Alpha-Amylase with superior thermal and low pH stability, HTA-430 has found its wide application in the production of starch sugar. (bolibio.com)
- Recent discoveries of starch degrading enzymes have led to increased application of amylases in various industrial processes (1). (scielo.br)
- The c-amylase (1,4-a-D-glucan glucanohydrolase, EC 3.2.1.1) hydrolyses a1,4 glucosidic linkages in starch and related substrates (5,18,23). (scielo.br)
- α-Amylase hydrolyzes the polysaccharides starch, malto-oligosaccharides at the α- d -(1,4)-glucosidic linkages to α-anomeric products. (sigmaaldrich.id)
- It is an endoamylase that can efficiently decrease viscosity of gelatinous starch solutions by randomly hydrolyzing starch, glycogen and its degradation products within the alpha-D-1 glycosidic bonds and produces soluble dextrins and oligosaccharides under high temperature and low pH conditions. (glucoamylaseenzyme.com)
- HA-800FG is an endoamylase which can rapidly decrease the viscosity of gelatinous starch solutions by randomly hydrolyzing starch, glycogen and its degradation products within the alpha-D-1,4 glucosidic bonds to produce soluble dextrins and oligosaccharides. (glucoamylaseenzyme.com)
- It is a kind of internal amylase, which can randomly hydrolyze starch, glycogen and their degradation products on α-Dmurl 4-glucoside bond into soluble dextrin and oligosaccharides, thus rapidly reducing the viscosity of colloidal starch solution. (glucoamylaseenzyme.com)
- Interacts directly with starch or other alpha-1,4-glucan. (joplink.net)
- One Unit of β-amylase activity is defined as the amount of enzyme required to release one µmole of maltose reducing-sugar equivalents per minute from soluble starch (10 mg/mL) in sodium phosphate buffer (200 mM), pH 6.0 at 40°C. (neogen.com)
- Despite obviously low RS content in the raw milled rice, the RS content in the hot cooked rice of mutant RS111 was significantly higher than that of the wild type and common rice and, correspondingly, in vitro starch hydrolysis by porcine pancreatic alpha-amylase tends to be incomplete with low hydrolysis extent for the cooked mutant rice high in RS. (nih.gov)
- In the present study, the inhibitory effect of tannins isolated from the alcoholic extract of fruits of Terminalia chebula was evaluated for the first time with porcine pancreatic amylase and potato starch as substrate. (manipal.edu)
- The kinetics of Alfa-amylase on starch is zero order at room temperature (28 0 c) for the first 5 minutes. (who.int)
Bacillus13
- Purification and properties of β-amylase produced by Bacillus polymyxa . (scialert.net)
- Activation of Bacillus licheniformis α-amylase through a disorder to order transition of the substrate binding site mediated by a calcium-sodium-calcium metal triad. (scialert.net)
- Alpha-Amylase is made from Bacillus subtilis,through fermentation and extraction method. (joinedfortunechemical.com)
- Low-temperature α-amylase (AAL) is produced by submerged fermentation of Bacillus subtilis followed by purification and formulation. (joinedfortunechemical.com)
- HTA-430 is a low pH tolerated Heat-stable Alpha-Amylase produced from selected strains of Bacillus licheniformis through submerged fermentation and refining extraction processes. (bolibio.com)
- alpha-Amylase from Bacillus sp. (sigmaaldrich.id)
- Heat-stable Alpha-Amylase TH-18 is produced from strains of Bacillus licheniformis through submerged fermentation, extraction and refining process. (glucoamylaseenzyme.com)
- The alpha-amylase of Bacillus stearothermophilus Q8, previously isolated in our laboratory, was purified by ammonium sulfate precipitation and CM-sephadex chromatography. (tmu.edu.tw)
- Lin, HY & Tsay, SS 1987, ' Extracellular thermostable alpha-amylase from Bacillus stearothermophilus Q8 ', Zhonghua Minguo wei sheng wu ji mian yi xue za zhi = Chinese journal of microbiology and immunology , vol. 20, no. 4, pp. 327-338. (tmu.edu.tw)
- HA-800FG is a Heat-stable Alpha-amylase produced from strains of Bacillus licheniformis through submerged fermentation and refining extraction processes. (glucoamylaseenzyme.com)
- HA-580FG is a food-grade thermostable α-amylase extracted from Bacillus licheniformis by submerged fermentation and purification. (glucoamylaseenzyme.com)
- INTRODUCTION High-temperature alpha-amylase is made from the best strain of Bacillus licheniformis through deep fermentation and extraction technique. (enzymes.bio)
- A bacterial alpha-amylase derived from a self-cloned strain of Bacillus licheniformis blended with Glycerine. (matesratehomebrewsupplies.com.au)
Enzymes6
- The blocking group in BPNPG7 prevents hydrolysis of this substrate by exo -acting enzymes such as amyloglucosidase, α-glucosidase, and β-amylase. (megazyme.com)
- Amylase Enzyme is typically used by all-grain brewers to add to a high adjunct mash that may be low in enzymes to aid in converting starches into sugar. (hamiltonhops.com)
- Recent research with thermostable a-amylases has concentrated on the enzymes of thermophiles and extreme thermophiles (2,3,7,8,16,17,20) and little is known about the properties of the enzymes produced by these organisms. (scielo.br)
- I am interested in Heat Stable Alpha Amylase Enzymes HA-580FG High Concentration For Alcohol could you send me more details such as type, size, quantity, material, etc. (glucoamylaseenzyme.com)
- The alpha-amylase family of enzymes is used to produce maltodextrin. (novonorddarou.com)
- This is possible by inhibiting certain carbohydrate hydrolyzing enzymes like alpha-amylase. (manipal.edu)
Pancreatic1
- Carbohydrate binding sites in a pancreatic α-amylase-substrate complex derived from x-ray structure analysis at 2.1Ao resolution. (scialert.net)
Cortisol4
- They also provided saliva samples for cortisol and alpha-amylase (AA) prior to and 5, 20 and 40 min post-mTSST. (salimetrics.com)
- Comparing Dental Stress in New Child Patients and Returning Patients Using Salivary Cortisol, Immunoglobulin-A and Alpha- Amylase. (bvsalud.org)
- this study was aimed at comparing dental stress in children having their first dental visit to those returning for dental treatment using salivary biomarkers of stress including salivary cortisol (s- cortisol ), Immunoglobulin -A (s- IgA ) and alpha-amylase (s-α- amylase ). (bvsalud.org)
- Salivary cortisol , s- IgA and s-α- amylase concentrations were obtained by Enzyme-linked Immunosorbent Assay ( ELISA ). (bvsalud.org)
Beta-amylase1
- Beta-amylase activity. (joplink.net)
Granules1
- The proteins synthesized by parotid acinar cells are stored in large secretory granules whose composition includes α-amylase, leucine-rich parotid secretory protein (PSP), and proline-rich proteins (PRPs), in addition to multiple minor components 2-3 related to digestive and protective functions. (bvsalud.org)
Substrate3
- Protein engineering in the α-amylase family: Catalytic mechanism substrate specificity and stability. (scialert.net)
- Aliquots of diluted extract (containing α-amylase) were incubated with substrate mixture under defined conditions of pH, temperature, and time. (megazyme.com)
- When the substrate is cleaved by endo-acting α-amylase, the nitrophenyl oligosaccharide is immediately and completely hydrolyzed to p -nitrophenol and free glucose by the excess quantities of α-glucosidase present in the substrate mixture. (megazyme.com)
Fungal alpha2
- Fungal Alpha-amylase is extracted from the Aspergillus oryzae. (meteoricbiopharma.com)
- DESCRIPTION Fungal Alpha-Amylase FAA-280 is made from Non-GMO strains of Aspergillus oryzae by submerged fermentation and refining extraction process. (bolibio.com)
Bacterial3
- The analyzed samples were white wheat flour, white wheat flour to which fungal α-amylase had been added, milled malt, and fungal and bacterial enzyme preparations. (megazyme.com)
- Studies on the alpha-amylase production were carried out with a bacterial strain isolated from a soil sample. (scielo.br)
- Studies were made to characterise soluble Alfa-Amylase (Bacterial). (who.int)
Protein5
- is a protein family which inhibits mammalian alpha-amylases specifically, by forming a tight stoichiometric 1:1 complex with alpha-amylase. (wikipedia.org)
- Salivary α-Amylase (sAA) is one of the most plentiful components in saliva, accounting for 10-20% of the total protein content [ 1 ]. (opendentistryjournal.com)
- The anti-Alpha-Amylase Microplate Assay Kit Antibody, 100 Assays is a α- or alpha protein sometimes glycoprotein present in blood.This antibody needs to be stored at + 4°C in a fridge short term in a concentrated dilution. (assayspro.com)
- Moreover, AD patients showed reduced gene expression of α-amylase, but conversely increased protein levels of α-amylase as well as increased activity of the enzyme compared to non-demented controls. (nin.nl)
- The amounts of protein in the immobilized Alfa-amylase prepared at pH 8.3 and 7.0 were estimated by, Kjeldhal method, by the tryptophan content and from the difference in the amount of protein present in the original solution and that in the washings. (who.int)
Activity20
- The PHF is screened for the phytochemical screening, and then the antidiabetic activity is determined by alpha-amylase inhibition. (hindawi.com)
- In in vitro study, the result revealed polyherbal formulation in which hot water extract has the topmost inhibitory effect on alpha-amylase activity, ranging from 20.4% to 79.5% with an IC50 value of 48.98 ± 0.31 μ g/ml. (hindawi.com)
- Alpha amylase activity was increased in the presence of MnCl 2 , CoCl 2 , ZnCl 2 and CaCl 2 but decreased with ethylene diamine tetra-acetic acid (EDTA), copper sulphate and silver nitrate. (scialert.net)
- α-amylase activity in Salvadora oleides fruit. (scialert.net)
- Thermostable pullulanase and α-amylase activity from Clostridium thermosulfurogenes SV9 optimization of culture conditions for enzyme production. (scialert.net)
- Release and activity of bound β-amylase in germinating barley grain. (scialert.net)
- When liquid whole egg is pasteurised, the efficiency of the pasteurisation can be checked by measuring the reduction in the alpa-amylase activity. (lovibond.com)
- Measurement of α-amylase activity in white wheat flour, milled malt, and microbial enzyme preparations, using the ceralpha assay: Collaborative study. (megazyme.com)
- This study was conducted to evaluate the method performance of a rapid procedure for the measurement of α-amylase activity in flours and microbial enzyme preparations. (megazyme.com)
- amylase inhibitory activity in marine algae samples and Myrmecodia platytyrea . (sigmaaldrich.id)
- The activity the of partial purified alpha-amylase was to be protected by bovine serum albumin Ca2+ and Mg2+. (tmu.edu.tw)
- Effect of Coumarin on Proline, Malondialdehyde and Alpha Amylase Activity in Lens culinaris Medik. (kocaeli.edu.tr)
- The in vitro alpha-amylase inhibitory activity of the microencapsulated product is also investigated. (ugm.ac.id)
- The optimal conditions for microcapsules formation were selected based on the activity of microcapsules as inhibitors for the alpha-amylase enzyme, pointing out by the lowest number of IC 50 . (ugm.ac.id)
- Changes in thymidine kinase and alpha-amylase activity during isopro- " by J P. Whitlock, R Kaufman et al. (jax.org)
- Changes in thymidine kinase and alpha-amylase activity during isopro- terenol-stimulated dna synthesis in mouse salivary gland. (jax.org)
- Lastly, we observed increased, albeit not significant, load of periodic acid-Schiff positive PGB in the brain of AD patients, which correlated with increased α-amylase activity. (nin.nl)
- Hence the activity of Alfa-amylase was measured in terms of mg maltose released during first five minutes. (who.int)
- Alfa-amylase showed optimal activity at pH 6.0 Cyanogen bromide was prepared and was used to activate sephadex G200 at pH 11.5. (who.int)
- A sample of immobilized Alfa-amylase (prepared at pH 8.3) was tested thrice in 3 weeks for stability on usage and it retained 85 percent of its original activity. (who.int)
Inhibitors1
- This family of inhibitors has no action on plant and microbial alpha amylases. (wikipedia.org)
Heat-stable1
- The product is not as heat-stable as thermostable α-amylase, bringing the benefit of easy inactivation. (joinedfortunechemical.com)
Extracellular2
- Purification and properties of extracellular amylase from the hyperthermophilic archaeon Thermococcus profundus DT5432. (scialert.net)
- Purification and characterization of extracellular α-amylase produced by Lactobacillus maninotivorans LMG 18010T, an amylolytic lactic acid bacterium. (scialert.net)
Polysaccharides1
- We therefore investigated whether alpha (α)-amylase, an enzyme known to efficiently degrade polysaccharides in the gastrointestinal tract, is expressed in the hippocampal CA1/subiculum and if the expression is altered in AD patients. (nin.nl)
Synthesis5
- The addition of calcium (10 mM) or peptone (1%) and yeast extract (0.5%) to the mineral medium shortened the lag period and improved the growth and alpha-amylase synthesis. (scielo.br)
- The addition of glucose to the culture diminished greatly the synthesis of alpha-amylase, demonstrating that a classical glucose effect is operative in this organism. (scielo.br)
- The optimum temperature and initial medium pH for amylase synthesis by the organism were 50°C and 7.0 respectively. (scielo.br)
- The addition of glucose to the culture diminished greatly the synthesis of alpha-amylase. (scielo.br)
- Alpha-amylase ment and intrathecal IgM synthesis. (cdc.gov)
Assay3
- A new amylase assay reagent containing p -nitrophenyl α-D-maltoheptaoside (blocked) plus a thermostable α-glucosidase. (megazyme.com)
- Powder enzyme form (2000°L) is for use in AACC and ASBC α-amylase assay procedures (see E-BARBP). (neogen.com)
- For use in AACC and ASBC α-amylase assay procedures. (neogen.com)
Soluble1
- The activities of the Alfa-amylases immobilized at pH 8.3 and 7.0 were, 0.75 percent and 0.52 percent of the total soluble Alfa-amylase respectively. (who.int)
Wheat5
- Detection and partial characterization of two antigenetically distinct β-amylase in developing kernel of wheat. (scialert.net)
- amylase) (EC 3.2.1.1) is an endo-amylolytic enzyme that plays an important role in seed germination in wheat. (jscimedcentral.com)
- amylase in post-harvest wheat grains has a negative effect on wheat yield and end-products quality. (jscimedcentral.com)
- A wide range of studies have been carried out on wheat alpha amylase due to its important biological roles in post-harvest spouting. (jscimedcentral.com)
- The inhalable flour dust samples were further analyzed for alpha-amylase and wheat. (cdc.gov)
Cereals4
- Cereal β-amylase: Diversity of the β-amylase isoenzyme status with in cereals. (scialert.net)
- β-amylase in cereals: A study of the maize β-amylase system. (scialert.net)
- In General, the development of methods for measuring α-amylase is pioneered in the clinical chemistry field and then translated to other industries, such as the cereals and fermentation industries. (megazyme.com)
- This article describes many of the commonly used methods for measuring α-amylase in the cereals, food, and fermentation industries and discusses some of the advantages and limitations of each. (megazyme.com)
Brewing2
- As a very robust Alpha-Amylase with superior thermal and pH stability, HA-800FG is applied to brewing industry such as beer and alcohol. (glucoamylaseenzyme.com)
- I am interested in Food Grade Liquid Alpha Amylase Enzyme Brewing Sepia Brown Liquid Appearance could you send me more details such as type, size, quantity, material, etc. (glucoamylaseenzyme.com)
Purification2
- Purification and characterization of α-amylase from poplar leaves. (scialert.net)
- Purification and properties of a hyperthermo active α-amylase from the archaeobacterium Pyracoccus woesei. (scialert.net)
Inactivation1
- Saccharification reaction can be terminated by heating to 80°C and keeping for 10∼20 minutes, or reducing the pH value to below 4.0 so that inactivation of fungal amylase is achieved. (bolibio.com)
Biochemical2
- High purity α-Amylase HR Reagent - 4 vials for the measurement of α-amylase for research, biochemical enzyme assays and in vitro diagnostic analysis. (megazyme.com)
- Biochemical properties such as production of alpha-amylase, beta-glucosidase, tannase, antimicrobials (presumptive bacteriocin and H(2)O(2)-production), acidification and fermentation of the indigestible sugars raffinose and stachyose, were evaluated in vitro for selection of potential starter strains. (who.int)
Fermentation1
- Measurement of α-Amylase in Cereal, Food and Fermentation Products. (megazyme.com)
Isolation1
- Isolation and sequence analysis of α-amylase cDNA clone. (scialert.net)
Stability1
- at 90°C. The stability of alpha amylase was increased in the presence of CoCl 2 . (scialert.net)
Regulatory1
- Independent regulatory aspects and post transational modification of two β-amylase in rye. (scialert.net)
Family1
- α-Amylase belongs to glycosyl hydrolase family 13. (sigmaaldrich.id)
Tannins1
- Natural antioxidants observed in plants involve tannins, flavonoids, vitamin C (ascorbic acid), and vitamin E (alpha-tocopherol). (hindawi.com)