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, ...
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 ...
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 ...
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 ...
These hybrid alpha amylases had the N-terminus of the alpha amylase from B. amyloliquefaciens joined to the C-terminus of the ... a) an alpha-amylase that is the expression product of a mutated DNA sequence encoding an alpha-amylase, the mutated DNA ... b) an alpha-amylase that is the expression product of a mutated DNA sequence encoding an alpha-amylase, the mutated DNA ... The use of alpha amylases in detergent compositions was known in the prior art and alpha amylases falling within the definition ...
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 ...
To be used with Still Spirits Distillers Yeasts and when starch is used in your recipe.Note that our Alpha-Amylase, unlike ... Note that our Alpha-Amylase, unlike many others, can handle temperatures up to 110 °C (220°F) before denaturing. ... "Alpha Amylase Enzyme Sachets - 4g","public_title":null,"options":["Default Title"],"price":3000,"weight":5,"compare_at_price":0 ...
Cortisol and salivary alpha-amylase are secreted in response to outside pressure or tension. A part of the autonomic nervous ... Cortisol, salivary alpha-amylase and childrens perceptions of their social networks. Social Neuroscience, 2015; 11 (2): 164 ... Three samples of saliva were collected before, during and after the interview and cortisol and alpha-amylase levels were ... and responded by secreting more alpha-amylase," Flinn said. "Our study was in line with past research on stress, loneliness and ...
Alpha Amylase Enzyme (15 grams) This thermostable powdered alpha amylase enzyme is used for the the hydrolysis of long-chain ... Briess Distillers MaltThis malt has exceptionally high alpha amylase and diastatic power for maximum fermentable yield.Lovibond ...
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... and alpha-amylase (s-α-amylase). Additionally, the study was aimed at monitoring the change in stress in new patients as they ... Salivary alpha-amylase significantly increased in new patients while being seated in the dental chair. Returning patients had ... Salivary cortisol, s-IgA and s-α-amylase concentrations were obtained by Enzyme-linked Immunosorbent Assay (ELISA). RESULTS:. ... Comparing Dental Stress in New Child Patients and Returning Patients Using Salivary Cortisol, Immunoglobulin-A and Alpha- ...
The noncatalytic triad of alpha-amylases: A novel structural motif involved in conformational stability.. Proteins (2008) 70(2 ... Amino acid bulkiness defines the local conformations and dynamics of natively unfolded alpha-synuclein and tau.. Journal of the ... Defining long-range order and local disorder in native alpha-synuclein using residual dipolar couplings.. Journal of the ... Letter to the Editor: Backbone H-N, N, C-alpha, C and C-beta assignment of the 25 kDa peptide methionine sulfoxide reductase ...
The study included a questionnaire, and blood tests for total IgE; IgE specific to flour dust, wheat, and alpha-amylase; and ... The prevalences of IgE specific to wheat, inhalable flour dust, and alpha-amylase were higher in the higher-exposure group at ... The inhalable flour dust samples were further analyzed for alpha-amylase and wheat. ... and to alpha-amylase at the >/= 0.10 kU/L cutoff. In conclusion, a health hazard exists at the Sara Lee Bakery in Sacramento, ...
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Salivary alpha amylase-cortisol asymmetry in maltreated youth. Horm Behav. 2008 Jan. 53(1):96-103. [QxMD MEDLINE Link]. ... For example, salivary alpha-amylase (sAA) (a putative correlate of norepinephrine) and cortisol have been used to evaluate 2 ... de Vries-Bouw M, Jansen L, Vermeiren R, Doreleijers T, de Ven Pv, Popma A. Concurrent attenuated reactivity of alpha-amylase ...
Different polyphenolic components of soft fruits inhibit alpha-amylase and alpha-glucosidase. J Agric.Food Chem 4-6-2005;53: ...
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A quantitative evaluation of the hydrolysis of wheat starch using Termamyl, a thermostable alpha-amylase (endo-l,4-alpha-D- ... A quantitative evaluation of the hydrolysis of wheat starch using Termamyl, a thermostable alpha-amylase (endo-l,4-alpha-D- ... a thermostable alpha-amylase (endo-l,4-alpha-D-glucan, glucanohydrolase; EC 3.2.1.78), is reported. Data from the monitoring of ...
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Hence the activity of Alfa-amylase was measured in terms of mg maltose released during first five minutes. Alfa-amylase showed ... The immobilized Alfa-amylase (prepared at pH 8.3) was stable on storage for a period of 3 weeks at 4 0 C in 0.4M phosphate ... Alfa-amylase was coupled to cyanogen bromide activated Sephadex G200 at pH8.3 and 7.0. Coupling of the enzyme led to further ... 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 ...
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  • Cortisol and salivary alpha-amylase are secreted in response to outside pressure or tension. (sciencedaily.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)
  • Salivary alpha-amylase significantly increased in new patients while being seated in the dental chair. (bvsalud.org)
  • The kinetics of Alfa-amylase on starch is zero order at room temperature (28 0 c) for the first 5 minutes. (who.int)
  • In this study, we wanted to explore the association between children's personal social networks, as well as perceived social network size and density with biomarkers like cortisol and alpha-amylase that can indicate levels of stress in youth. (sciencedaily.com)
  • Three samples of saliva were collected before, during and after the interview and cortisol and alpha-amylase levels were measured. (sciencedaily.com)
  • We found that, using the data we collected from the one-on-one interviews, children who were stressed about the size and density of their perceived social networks had elevated anticipatory cortisol levels, and responded by secreting more alpha-amylase," Flinn said. (sciencedaily.com)
  • Influence of a 'warm touch' support enhancement intervention among married couples on ambulatory blood pressure, oxytocin, alpha amylase, and cortisol. (bvsalud.org)
  • The binding of tendamistat to alpha-amylase leads to the steric blockage of the active site of the enzyme. (wikipedia.org)
  • is a protein family which inhibits mammalian alpha-amylases specifically, by forming a tight stoichiometric 1:1 complex with alpha-amylase. (wikipedia.org)
  • 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 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)
  • The inhalable flour dust samples were further analyzed for alpha-amylase and wheat. (cdc.gov)
  • For instance, in wheat, more than 40 water soluble allergens have been described [11±13], whereas commercially available fungal a-amylase ex- tracts contain one major allergen, Asp o II, and one or two other components to which workers can develop IgE antibodies [14,15]. (cdc.gov)
  • Returning patients had higher s-α- amylase (p=0.001) and s- IgA (p=0.016) compared to new patients . (bvsalud.org)
  • 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)
  • 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)
  • These new enzymes are replacing alpha-amylase in several applications because of their lower viscosity. (globenewswire.com)
  • Amylases are enzymes that catalyze the hydrolysis of amylopectin, amylose, glycogen, and their hydrolyzed products into simple and easily digestible sugars. (medscape.com)
  • For α- amylase and sorbitol dehydrogenase enzymes , IC50 values were 25.03 and 1.47 µM. (bvsalud.org)
  • Comparison of stored and secreted rat pancreatic digestive enzymes by mass spectrometry: alpha-amylase. (nih.gov)
  • Alpha-amylase enzymes are specifically designed to facilitate starch utilisation and availability, providing more energy to the cow. (dairyglobal.net)
  • The next part of this book focuses on the structure of various enzymes found in B. subtilis, including alpha amylases, subtilisin, alkaline phosphatase, and levansucrase. (elsevier.com)
  • Plasma samples that have been anticoagulated with citrate or oxalate should be avoided because amylase is a calcium-containing enzyme and false low levels can be obtained with such specimens. (medscape.com)
  • The alpha-amylase expressed in E. Coli exhibited the temperature-dependent activation characteristic of the original enzyme from P. furiosus, but had a higher apparent molecular weight that was attributed to the improper formation of the native quaternary structure. (nih.gov)
  • It also contains the enzyme, Alpha-Amylase which breaks down starches, improving the animal's digestive performance. (medicanimal.com)
  • Supplementation with an alpha-amylase enzyme such as Amaize may further improve productivity by enhancing digestion at the microbial level. (dairyglobal.net)
  • Research on the alpha-amylase enzyme technology Amaize has shown promise in not only changing starch digestion but also modifying overall ruminal digestion, optimising overall nutrient utilisation and boosting feed efficiency and milk production. (dairyglobal.net)
  • By providing a different mix of oligosaccharides than would be available without enzyme supplementation, alpha-amylase allows different rumen microbes to proliferate. (dairyglobal.net)
  • Several commercial and university research studies have addressed the effects and benefits of alpha-amylase enzyme technologies such as Amaize in dairy rations. (dairyglobal.net)
  • Supplementation with the alpha-amylase enzyme improved average milk production (by 1.3 kg), fat-corrected milk production, milk fat yield and milk protein yield across the eight herds studied. (dairyglobal.net)
  • 2005) examined the effects of alpha-amylase enzyme technology on rumen fermentation and milk production in lactating Holsteins. (dairyglobal.net)
  • Research into alpha-amylase enzyme technology has continued with a recent publication from Bugoni et al . (dairyglobal.net)
  • 2023), reporting that cows supplemented with a combination of an alpha-amylase enzyme (Amaize) and a proteolytic enzyme (Vegpro) digested the starch in their feed more completely. (dairyglobal.net)
  • An increase in milk yield was also seen for cows given this alpha-amylase/proteolytic enzyme combination, as well as for cows given only the alpha-amylase. (dairyglobal.net)
  • 2007) reported that when supplementing Holstein bull calves with the alpha-amylase enzyme in the calf starter from birth through 5 weeks of age, amylase led to enhanced rumen tissue growth. (dairyglobal.net)
  • Determination of alpha-amylase inhibitor activity of phaseolamin from kidney bean (Phaseolus vulgaris) in dietary supplements by HPAEC-PAD. (nih.gov)
  • The highest activity of amylase, lipase and protease (4.43, 73.2 and 2071.3 unit mg -1 protein, respectively) observed in hormone priming and non-stress conditions. (ac.ir)
  • The lowest amylase activity (3.1 unit mg -1 protein) was related to osmo-priming and -9 bar drought while the lowest activity of lipase and protease (60.36 and 1949 unit mg -1 protein, respectively) observed in -9 bar drought in non-primed seeds. (ac.ir)
  • This is not the case, however, for Bacillus licheniformis alpha-amylase (BLA) for which the structure of the metal-free form is available. (nih.gov)
  • 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)
  • 1984. Mathematical models of depolymerization of amylose by alpha-amylases . (ibpc.fr)
  • 3. Kinetic aspects of alkaline phosphatase refolding in the presence of alpha-cyclodextrin. (nih.gov)
  • Consumption of the alpha-amylase inhibitor causes marginal intraluminal alpha-amylase activity facilitated by the inhibitor's appropriate structural, physico-chemical and functional properties. (nih.gov)
  • The efficacy and safety of the amylase inhibitor extracts, however, depend on the processing and extraction techniques used. (nih.gov)
  • In this article, Anfinsen, et al, reported that while trying to study the factors that influenced protein thermostability, or the ability to remain stable at relatively high temperatures, they had cloned a gene from the hyperthermophilic bacterium Pyrococcus furiosus encoded with a highly thermostable alpha-amylase and expressed it in Escherichia Coli. (nih.gov)
  • 7. Protein refolding assisted by molecular tube based alpha-cyclodextrin as an artificial chaperone. (nih.gov)
  • Macroamylasemia is a condition of persistently elevated serum amylase activity with no apparent pancreatic disorder due to the formation of a large amylase-globulin complex, which is not excreted. (medscape.com)
  • Serum amylase increases in 6-48 hrs of onset of acute pancreatitis but not in proportion to the severity of the disease and activity returns to normal in 3-5 days. (medscape.com)
  • The ratio of amylase urinary clearance to creatinine clearance can be used in the diagnosis of acute and relapsing pancreatitis. (medscape.com)
  • 19. Artificial chaperone-assisted refolding of GuHCl-denatured alpha-amylase at low temperature: refolding versus aggregation. (nih.gov)
  • Urine amylase increases in proportion to serum amylase and remains elevated for several days after serum amylase has been normalized. (medscape.com)
  • The chemical activities of violanthin against alpha amylase and sorbitol dehydrogenase were investigated utilizing the molecular docking study. (bvsalud.org)
  • ChBP comprises a beta sandwich domain and an (alpha/alpha)(6) barrel domain, constituting a distinctive structure among GT families. (embl.de)
  • The structure shows that the calcium-binding site which is conserved in all alpha-amylases forms part of an unprecedented linear triadic metal array, with two calcium ions flanking a central sodium ion. (nih.gov)
  • Amylase molecule from human saliva. (medscape.com)
  • We made more of the human alpha-amylase gene insert (obtained from Integrated DNA Technologies) through PCR amplification. (igem.wiki)
  • The human alpha-amylase gene insert (GOI) appeared to be in the right location-between 1000bp-1500bp in length. (igem.wiki)
  • In Silico Studies, Anti-oxidant Properties, Antisorbitol Dehydrogenase, Anti-alpha Amylase and Anti-gastrointestinal Cancer Potential of Violanthin as a Natural Compound. (bvsalud.org)
  • Timed urine specimens can be obtained for urinary amylase and normalized to creatinine content. (medscape.com)
  • Most elevations in serum amylase are due to increased rates of amylase entry into the blood stream, decreased rates of clearance or both. (medscape.com)