A subclass of alpha-amylase ISOENZYMES that are secreted into SALIVA.
A group of amylolytic enzymes that cleave starch, glycogen, and related alpha-1,4-glucans. (Stedman, 25th ed) EC 3.2.1.-.
Enzymes that catalyze the endohydrolysis of 1,4-alpha-glycosidic linkages in STARCH; GLYCOGEN; and related POLYSACCHARIDES and OLIGOSACCHARIDES containing 3 or more 1,4-alpha-linked D-glucose units.
Increased salivary flow.
The clear, viscous fluid secreted by the SALIVARY GLANDS and mucous glands of the mouth. It contains MUCINS, water, organic salts, and ptylin.
A nodular organ in the ABDOMEN that contains a mixture of ENDOCRINE GLANDS and EXOCRINE GLANDS. The small endocrine portion consists of the ISLETS OF LANGERHANS secreting a number of hormones into the blood stream. The large exocrine portion (EXOCRINE PANCREAS) is a compound acinar gland that secretes several digestive enzymes into the pancreatic ductal system that empties into the DUODENUM.
The largest of the three pairs of SALIVARY GLANDS. They lie on the sides of the FACE immediately below and in front of the EAR.
Plasma glycoprotein member of the serpin superfamily which inhibits TRYPSIN; NEUTROPHIL ELASTASE; and other PROTEOLYTIC ENZYMES.

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.

In molecular biology, alpha-amylase inhibitor (or α-...) is a protein family which inhibits mammalian alpha-amylases ... 1 complex with alpha-amylase. This family of inhibitors has no action on plant and microbial alpha amylases. A crystal ... The binding of tendamistat to alpha-amylase leads to the steric blockage of the active site of the enzyme. The crystal ... König V, Vértesy L, Schneider TR (October 2003). "Structure of the alpha-amylase inhibitor tendamistat at 0.93 A". Acta ...
The alpha-Amylase Protein alpha-Amylase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) This article ... See amylase for more uses of the amylase family in general. α-Amylase has exhibited efficacy in degrading polymicrobial ... Medical laboratories will usually measure either pancreatic amylase or total amylase. If only pancreatic amylase is measured, ... "Amylase, Alpha - Worthington Enzyme Manual". worthington-biochem.com. Archived from the original on 14 October 2016. Valls, ...
4-alpha-D-glucan 4-alpha-D-glucosyltransferase. Other names in common use include amylase III, and 1,4-alpha-glucan:1,4-alpha- ... glucan 4-alpha-glucosyltransferase. Nebinger P (March 1986). "Separation and characterization of four different amylases of ... 4-alpha-D-glucan to the 4-position of an alpha-D-glucan. This enzyme is useful in hydrolyzing oligosaccharides. This enzyme ... Characterization of amylases". Biological Chemistry Hoppe-Seyler. 367 (3): 169-76. doi:10.1515/bchm3.1986.367.1.169. PMID ...
The pancreas and salivary gland make amylase (alpha amylase) to hydrolyse dietary starch into disaccharides and trisaccharides ... Both α-amylase and β-amylase are present in seeds; β-amylase is present in an inactive form prior to germination, whereas α- ... In human physiology, both the salivary and pancreatic amylases are α-amylases. The α-amylase form is also found in plants, ... "Amylase, Alpha, I.U.B.: 3.2.1.11,4-α-D-Glucan glucanohydrolase". Wadler J (8 September 2009). "Chew It Up, Spit It Out, Then ...
"Amylase, Alpha" , I.U.B.: 3.2.1.11,4-α-D-Glucan glucanohydrolase. "Amylase, Alpha" , I.U.B.: 3.2.1.11,4-α-D-Glucan ... The optimum pH for β-amylase is 4.0-5.0 They belong to Glycoside hydrolase family 14. Amylase Alpha-amylase Rejzek M, Stevenson ... "Amylase, Alpha" , I.U.B.: 3.2.1.11,4-α-D-Glucan glucanohydrolase. Friedberg F, Rhodes C (March 1986). "Cloning and ... β-Amylase (EC 3.2.1.2, saccharogen amylase, glycogenase) is an enzyme with the systematic name 4-α-D-glucan maltohydrolase. It ...
Richardson M, Bloch Jr C (1991). "A new family of small (5 kDa) protein inhibitors of insect alpha-amylases from seeds or ... Inhibitors of insect alpha-amylases from sorghum. Probable protease inhibitor P322 from Solanum tuberosum (potato). A ... "Plant α-amylase inhibitors and their interaction with insect α-amylases: Structure, function and potential for crop protection ... Some plant defensins have also been identified as enzyme inhibitors of α-amylase or trypsin. It is believed that these are ...
... maltogenic alpha-amylase, 1,4-alpha-D-glucan alpha-maltohydrolase) is an enzyme with systematic name 4-alpha-D-glucan alpha- ... alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose residues from the non-reducing ends of ... Glucan+1,4-alpha-maltohydrolase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC ... Maltogenic amylases from Bacillus stearothermophilus, Thermus sp. and Geobacillus thermoleovorans are able to degrade acarbose ...
The human AMY1C gene encodes the protein Amylase, alpha 1C (salivary). Amylases are secreted proteins that hydrolyze 1,4-alpha- ... "Entrez Gene: Amylase, alpha 1C (salivary)". Retrieved 2013-02-14. [provided by RefSeq, Jul 2008]. ##RefSeq-Attributes-START## ... This gene encodes an amylase isoenzyme produced by the salivary gland. See also Amylase § Evolution. GRCh38: Ensembl release 89 ... Human Alpha-amylase 1) at the PDBe-KB. v t e (Articles with short description, Short description matches Wikidata, Genes on ...
Murao, Sawao; Oouchi, Naoki; Goto, Akira; Arai, Motoo (1983). "New proteinaceous .ALPHA.-amylase inhibitor (Paim) from ...
Some salivary components are crucial for plaques ecosystem, such as salivary alpha-amylase which plays a role in binding and ... Scannapieco FA, Torres G, Levine MJ (1993). "Salivary alpha-amylase: role in dental plaque and caries formation". Critical ...
Organisms can either by alpha-hemolytic, beta-hemolytic, or gamma-hemolytic (non-hemolytic). Amylases are a group of ... The different classes of amylases are α-amylases, β-amylases, and glucoamylases. The α-amylases hydrolyze starch by randomly ... Sharma A, Satyanarayana T (2013). "Microbial acid-stable alpha-amylases: Characteristics, genetic engineering and applications ... Amylase breaks down carbohydrates into mono- and disaccharides, so a starch agar must be used for this assay. Once the bacteria ...
Alpha-amylase 2B is an enzyme that in humans is encoded by the AMY2B gene. Amylases are secreted proteins that hydrolyze 1,4- ... "Entrez Gene: AMY2B amylase, alpha 2B (pancreatic)". Human AMY2B genome location and AMY2B gene details page in the UCSC Genome ... Koyama I, Komine S, Iino N, Hokari S, Igarashi S, Alpers DH, Komoda T (July 2001). "alpha-Amylase expressed in human liver is ... Groot PC, Bleeker MJ, Pronk JC, Arwert F, Mager WH, Planta RJ, Eriksson AW, Frants RR (July 1989). "The human alpha-amylase ...
Without alpha-amylase, yeast would not be able to ferment. Maltose-glucoamylase is commonly used as a fermentation source as it ... alpha-D-glucosidase, alpha-glucoside hydrolase, alpha-1,4-glucosidase, alpha-D-glucoside glucohydrolase) is one type of alpha- ... Alpha-amylase 1 which is coded on the AMY1A gene is responsible of cleaving α-glucosidase linkages in oligosaccharides and ... The rate of hydrolysis is controlled by the size of the substrate (carbohydrate size). Alpha-amylase has an important function ...
There it is broken down into oligosaccharides by the enzyme alpha-amylase. In patients with intact kidney function, both ...
Their catalyses are similar to that of alpha-amylase and glucoamylase, respectively. Their active sites are selective towards ... In E. coli, Glucose transfer is performed by 4-alpha-glucanotransferase, a 78.5 kDa protein coded for by the gene malQ. A ... "4-alpha-glucanotransferase - Escherichia coli (strain K12)". "Glycogen debranching enzyme - Escherichia coli O139:H28 (strain ... Yamamoto E, Makino Y, Omichi K (May 2007). "Active site mapping of amylo-alpha-1,6-glucosidase in porcine liver glycogen ...
1988). "Primary structure of human pancreatic alpha-amylase gene: its comparison with human salivary alpha-amylase gene". Gene ... Alpha-amylase 1 is an enzyme that in humans is encoded by the AMY1A gene. This gene is found in many organisms. Amylases are ... "Entrez Gene: AMY1A amylase, alpha 1A; salivary". Human AMY1A genome location and AMY1A gene details page in the UCSC Genome ... 1989). "The human alpha-amylase multigene family consists of haplotypes with variable numbers of genes". Genomics. 5 (1): 29-42 ...
1994). "The active center of a mammalian alpha-amylase. Structure of the complex of a pancreatic alpha-amylase with a ... 1988). "Primary structure of human pancreatic alpha-amylase gene: its comparison with human salivary alpha-amylase gene" (PDF ... Pancreatic alpha-amylase is an enzyme that in humans is encoded by the AMY2A gene. Amylases are secreted proteins that ... "Entrez Gene: AMY2A amylase, alpha 2A; pancreatic". Human AMY2A genome location and AMY2A gene details page in the UCSC Genome ...
However, bacterial alpha-amylases from gut microbiome are able to degrade acarbose. Pancreatic alpha-amylase hydrolyzes complex ... October 2007). "The 'pair of sugar tongs' site on the non-catalytic domain C of barley alpha-amylase participates in substrate ... It has been reported that the maltogenic alpha-amylase from Thermus sp. IM6501 (ThMA) and a cyclodextrinase (CDase) from ... Human enzymes do transform acarbose: the pancreatic alpha-amylase is able to perform a rearrangement reaction, moving the ...
One of the outcomes of this research was the use of alpha-amylase gene promoters to express human proteins in transgenic rice ... Sequence-specific interactions of a nuclear protein factor with the promoter of a rice gene for alpha-amylase, RAamy3D.. Nucl. ... Metabolic regulation of rice alpha-amylase and sucrose synthase genes in planta. The Plant Journal, 2(4):517-523. Huang, N., ... Organization, structure and expression of the rice alpha-amylase multigene family. In, Rice Genetics II. Manila, pp. 417-429. ...
It is mainly used in assay of alpha-amylase. However, enzymatic methods are usually preferred due to DNS's lack of specificity ...
They can be digested by breaking the alpha-linkages (glycosidic bonds). Both humans and other animals have amylases so that ... Starch is a glucose polymer in which glucopyranose units are bonded by alpha-linkages. It is made up of a mixture of amylose ( ... This carbohydrate can react with water (hydrolysis) using amylase enzymes as catalyst, which produces constituent sugars ( ...
Also said to be the source of Tendamistat (HOE 467), an alpha amylase inhibitor. Dionigi, Christopher P.; Ingram, Daphne A. ( ...
If it has occurred, there is a dramatic increase of the enzyme alpha-amylase. The Falling Number test is a measure of the ... In bread, too much alpha-amylase activity will cause wet sticky bread crumb with large voids in the loaf and too little causes ...
MacGregor EA, Jespersen HM, Svensson B (January 1996). "A circularly permuted alpha-amylase-type alpha/beta-barrel structure in ... have a different arrangement than those in α-amylase. The folding characteristics of α-amylase and glucansucrase are still very ... However, glucansucrase is very similar to α-amylase, another sugar-cutting enzyme. Glucansucrase thus has many of the same ... Glucansucrase proteins likely evolved from an amylase enzyme precursor. The two enzymes have similar folding patterns and ...
"Nucleotide sequence and expression of a Streptomyces griseosporeus proteinaceous alpha-amylase inhibitor (HaimII) gene". ... "Molecular cloning and expression in Streptomyces lividans of a proteiunous α-amylase inhibitor (HaimII) gene from Streptomyces ...
... amylase (amylo). Alpha amylase from B. amyloliquefaciens is often used in starch hydrolysis. It is also a source of subtilisin ... J. Fukumoto (1943). "Studies on the production of bacterial amylase. I. Isolation of bacteria secreting potent amylases and ...
Additionally, the alpha amylase has been suggested to prevent bacterial attachment to oral surfaces and to enable bacterial ... The parotid gland also secretes salivary alpha-amylase (sAA), which is the first step in the decomposition of starches during ... With the inflammation of mumps or obstruction of the ducts, increased levels of the salivary alpha amylase secreted by the ... ISBN 978-1-4377-1730-3. Arhakis A, Karagiannis V, Kalfas S (2013). "Salivary alpha-amylase activity and salivary flow rate in ...
... its alpha 1-4 linkages having already been broken down by amylase). The product of the enzymatic digestion of alpha-limit ... Isomaltase helps amylase to digest alpha-limit dextrin to produce maltose. The human sucrase-isomaltase is a dual-function ... It digests polysaccharides at the alpha 1-6 linkages. Its substrate, alpha-limit dextrin, is a product of amylopectin digestion ... and oligosaccharide alpha-1,6-glucohydrolase. This enzyme catalyses the following chemical reaction Hydrolysis of (1->6)-alpha- ...
Buisson G, Duée E, Haser R, Payan F (December 1987). "Three dimensional structure of porcine pancreatic alpha-amylase at 2.9 A ... 4-alpha-D-glucan:1,4-alpha-D-glucan 6-alpha-D-(1,4-alpha-D-glucano)-transferase. Other names in common use include branching ... 4-alpha-glucan branching enzyme 1, plant branching enzyme, alpha-1,4-glucan:alpha-1,4-glucan-6-glycosyltransferase, and starch ... Glycogen branching enzyme belongs to the α-amylase family of enzymes, which include α-amylases, pullulanas/isoamylase, ...
doi:10.1007/978-3-642-27603-3_5. ISBN 978-3-642-27602-6. Williams LK, Brayer GD (2015-11-25). "Porcine pancreatic alpha-amylase ... The alpha defensin peptides are increased in chronic inflammatory conditions. Alpha defensin are increased in several cancers, ... "Novel insights on the mechanism of action of alpha-amylase inhibitors from the plant defensin family". Proteins. 73 (3): 719-29 ... Only alpha and beta-defensins are expressed in humans. Although the most well-studied defensins are from vertebrates, a family ...
In molecular biology, alpha-amylase inhibitor (or α-...) is a protein family which inhibits mammalian alpha-amylases ... 1 complex with alpha-amylase. This family of inhibitors has no action on plant and microbial alpha amylases. A crystal ... The binding of tendamistat to alpha-amylase leads to the steric blockage of the active site of the enzyme. The crystal ... König V, Vértesy L, Schneider TR (October 2003). "Structure of the alpha-amylase inhibitor tendamistat at 0.93 A". Acta ...
ALPHA-AMYLASECALCIUM IONSULFATE IONalpha-D-glucopyranose
The PHF is screened for the phytochemical screening, and then the antidiabetic activity is determined by alpha-amylase ... the result revealed polyherbal formulation in which hot water extract has the topmost inhibitory effect on alpha-amylase ... of inhibition can be expressed by the inhibition of alpha-amylase and calculated by a formula which is given as follows:. ... Assessment of Antioxidative and Alpha-Amylase Potential of Polyherbal Extract. Mohsina Patwekar. ,1Faheem Patwekar. ,1Amine ...
Fungal. Granules. Breaks starch into the form of maltose. Commercial-grade enzyme. May be stored at 5° C for up to 1 year without appreciable loss of activity. Comes with (M)SDS and Introduction to Enzymes booklet. 100-g bottle.
alpha-amylase Women Who Worry A Lot Are Less Likely To Give Birth To Baby Boys. October 17, 2011. by Affleap ... Categories Parenting Tags adrenaline, alpha-amylase, babies, boys, cortisol, girls, Lifestyle, parents, pregnancies, stress, ...
... of the Alpha Amylase from Moringa oleifera Seeds ... Properties of the Alpha Amylase from Moringa oleifera Seeds ... at 90°C. The stability of alpha amylase was increased in the presence of CoCl2. Alpha amylase activity was increased in the ... Properties of the Alpha Amylase from Moringa oleifera Seeds. Journal of Biological Sciences, 1: 747-749. DOI: 10.3923/jbs. ... Crude alpha amylase preparation from Moringa oleifera seeds was used to hydrolyze starch. The enzyme has maximum activity at pH ...
Hypothesis that alpha-amylase evokes regulatory mechanisms originating in the pancreas, gut and circulation, which govern ... alpha-amylase were much higher than physiological alpha-amylase levels and thus could possibly have increased the alpha-amylase ... Alpha-amylase synthesis is extraordinarily stimulated by insulin-halo phenomenon. In turn, alpha-amylase, through its ability ... The more physiological mechanism, however, would be the direct action of alpha-amylase or alpha-amylase-derived peptides on gut ...
Behavior problems in youth may show a higher salivary cortisol - alpha amylase coordination. ... They also provided saliva samples for cortisol and alpha-amylase (AA) prior to and 5, 20 and 40 min post-mTSST. Analyses ...
... the efficiency of the pasteurisation can be checked by measuring the reduction in the alpa-amylase activity. ... Alpha Amylase Activity in Liquid Egg When liquid whole egg is pasteurised, the efficiency of the pasteurisation can be checked ...
Alpha-glucosidase and alpha-amylase inhibiting thiodiketopiperazines from the endophytic fungus Setosphaeria rostrata isolated ... Alpha-glucosidase and alpha-amylase inhibiting thiodiketopiperazines from the endophytic fungus Setosphaeria rostrata isolated ... Alpha-glucosidase and alpha-amylase inhibiting thiodiketopiperazines from the endophytic fungus Setosphaeria rostrata isolated ...
Purchase high purity alpha-Amylase HR Reagent for the measurement of alpha-amylase for research biochemical enzyme assays and ... K-CERA - α-Amylase Assay Kit (Ceralpha Method). K-AMYLSD - α-Amylase SD Assay Kit K-MALTA - Malt Amylase Assay Kit ... E-ANAAM - α-Amylase (Aspergillus oryzae) E-BLAAM-40ML - α-Amylase (Bacillus licheniformis) E-PANAA-12G - α-Amylase (Porcine ... High purity α-Amylase HR Reagent - 4 vials for the measurement of α-amylase for research, biochemical enzyme assays and in ...
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 ...
... amylase) (EC 3.2.1.1) is an endo-amylolytic enzyme that plays an important role in seed germination in wheat. However, ... Alpha amylase (?-amylase) (EC 3.2.1.1) is an endo-amylolytic enzyme that plays an important role in seed germination in wheat. ... A wide range of studies have been carried out on wheat alpha amylase due to its important biological roles in post-harvest ... However, excessive ?-amylase in post-harvest wheat grains has a negative effect on wheat yield and end-products quality. ...
Alpha Amylase. What is Alpha Amylase?. Alpha amylase is the major form of amylase found in humans and other mammals. [1]. ... "Alpha Amylase".. The data is calculated from UPC Food Searchs product data only, and is not meant to reflect all food products ...
A detailed product description will follow - this section is currently under construction. Please refer to the basic product description for general information about this product/device. Thank you for your patience!
Fungal Alpha-amylase is extracted from the Aspergillus oryzae.. *Fungal Diastase (fungal alpha amylase) has both liquefying and ...
Alpha-Amylase is made from Bacillus subtilis,through fermentation and extraction method. This product can hydrolyze starch into ... Low-temperature α-amylase (AAL) is produced by subme ... What is Alpha Amylase ?. Alpha-Amylase is made from Bacillus ... Low-temperature α-amylase (AAL) is produced by submerged fermentation of Bacillus subtilis followed by purification and ... The product is not as heat-stable as thermostable α-amylase, bringing the benefit of easy inactivation.. The enzyme is widely ...
Alpha-Amylase is a bacterial-derived enzyme that breaks down starch into dextrins and simple sugars during mashing. Bring your ... Alpha-Amylase is a bacterial-derived enzyme that breaks down starch into dextrins and simple sugars during mashing. ... var _learnq = _learnq ,, []; var item = { Name: "Still Spirits Distillers Alpha-Amylase Enzyme", ProductID: 7009057505395, ... brewsrq.com/cdn/shop/products/still-spirits-distiller-s-alpha-amylase-enzyme-31018650894451_grande.jpg?v=1666280432", URL: " ...
Be the first to review "Alpha-Amylase Enzyme" Cancel reply. Your email address will not be published. Required fields are ... Thermostable powdered alpha-amylase enzyme for hydrolysis of long-chain starch molecules into short-chain dextrins. For use in ...
Fungal Alpha-Amylase FAA-280 DESCRIPTION Fungal Alpha-Amylase FAA-280 is made from Non-GMO strains of Aspergillus oryzae by ... DESCRIPTION Fungal Alpha-Amylase FAA-280 is made from Non-GMO strains of Aspergillus oryzae by submerged fermentation and ... Fungal Alpha-Amylase FAA-280 is made from Non-GMO strains of Aspergillus oryzae by submerged fermentation and refining ... In the production of malt syrup, first use heat-stable alpha-amylase for starch liquefaction so that DE value of the liquefied ...
Alpha-Amylase is a bacterial-derived enzyme which breaks down starch into dextrins and simple sugars during mashing. Good up to ...
HTA-430 is a low pH tolerated Heat-stable Alpha-Amylase widely used in the production of starch sugar. ... As a robust Alpha-Amylase with superior thermal and low pH stability, HTA-430 has found its wide application in the production ... HTA-430 is a low pH tolerated Heat-stable Alpha-Amylase widely used in the production of starch sugar. ... HTA-430 is a low pH tolerated Heat-stable Alpha-Amylase produced from selected strains of Bacillus licheniformis through ...
AMY2, 1,4-alpha-D-glucan glucanohydrolase,alpha-amylase carcinoid,amylase, pancreatic, alpha-2B,glycogenase. ...
Studies on the alpha-amylase production were carried out with a bacterial strain isolated from a soil sample. The cells were ... The addition of glucose to the culture diminished greatly the synthesis of alpha-amylase, demonstrating that a classical ... to the mineral medium shortened the lag period and improved the growth and alpha-amylase synthesis. ... The addition of glucose to the culture diminished greatly the synthesis of alpha-amylase. ...
Background: Endohydrolysis of (1-,4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1-,4)-alpha- ...
Usage varies. 1tsp. Breaks 1,4 linkage in starch during liquefication, producing dextrin and a small amout of maltose.. Leaves 1,6 links, therefore self-limiting. Use if you have a starch problem in storage, or in light beers. ...
Correlating Molecular Interactions with Solubility of Alpha-Amylase from Bacillus Licheniformis. C.M. Mehta, E.T. White, J.D. ... Mehta CM, White ET, Lister JD, Hardin M, Lenhoff A. Correlating Molecular Interactions with Solubility of Alpha-Amylase from ... Correlating Molecular Interactions with Solubility of Alpha-Amylase from Bacillus Licheniformis. / Mehta, C.M.; White, E.T.; ... Correlating Molecular Interactions with Solubility of Alpha-Amylase from Bacillus Licheniformis - Salt Lake City, USA. Duration ...
Amylase from Bacillus sp. has been used in the digestion of lyophilized microalgae sample.. It has also been used to evaluate α ... α-Amylase belongs to glycosyl hydrolase family 13.. It comprises of A, B and C domains. Domain A has two aspartic acid and a ... α-Amylase hydrolyzes the polysaccharides starch, malto-oligosaccharides at the α-. d. -(1,4)-glucosidic linkages to α-anomeric ...
... with strict quality control textile alpha amylase enzyme factories, producing high quality low dosage rate alpha amylase enzyme ... Chinas leading liquid desizing alpha amylase enzyme product, ... High quality Liquid Desizing Textile Alpha Amylase Enzyme With ... Beige Yellow Alpha Amylase Enzyme Powder , Heat - Stable Enzyme Alpha Amylase. * High Concentration Alpha Amylase Enzyme 40000 ... liquid desizing alpha amylase enzyme. , textile alpha amylase enzyme. , low dosage rate alpha amylase enzyme. ...
title = "Extracellular thermostable alpha-amylase from Bacillus stearothermophilus Q8",. abstract = "The alpha-amylase of ... Extracellular thermostable alpha-amylase from Bacillus stearothermophilus Q8. / Lin, H. Y.; Tsay, S. S. In: Zhonghua Minguo wei ... Extracellular thermostable alpha-amylase from Bacillus stearothermophilus Q8. Zhonghua Minguo wei sheng wu ji mian yi xue za ... Lin, H. Y. ; Tsay, S. S. / Extracellular thermostable alpha-amylase from Bacillus stearothermophilus Q8. In: Zhonghua Minguo ...
  • 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)
  • 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)
  • 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)
  • Carbohydrate binding sites in a pancreatic α-amylase-substrate complex derived from x-ray structure analysis at 2.1Ao resolution. (scialert.net)
  • 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)
  • 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)
  • 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 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)
  • 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)
  • 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)
  • 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)
  • This family of inhibitors has no action on plant and microbial alpha amylases. (wikipedia.org)
  • The product is not as heat-stable as thermostable α-amylase, bringing the benefit of easy inactivation. (joinedfortunechemical.com)
  • 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)
  • 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)
  • 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)
  • 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)
  • 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)
  • 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)
  • 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)
  • 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)
  • 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)
  • 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)
  • 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)
  • Measurement of α-Amylase in Cereal, Food and Fermentation Products. (megazyme.com)
  • Isolation and sequence analysis of α-amylase cDNA clone. (scialert.net)
  • at 90°C. The stability of alpha amylase was increased in the presence of CoCl 2 . (scialert.net)
  • Independent regulatory aspects and post transational modification of two β-amylase in rye. (scialert.net)
  • Natural antioxidants observed in plants involve tannins, flavonoids, vitamin C (ascorbic acid), and vitamin E (alpha-tocopherol). (hindawi.com)