Cleanup date October 2008 Refimprove date July 2009 Image Salivary alpha amylase 1SMD.png thumb A diagram of an amylase molecule from human saliva. Calcium ion visible in pale khaki chloride ion in green. From PDB 1SMD . Image Pancreatic alpha amylase 1HNY.png thumb Human pancreatic amylase. Calcium ion visible in pale khaki chloride ion in green. From PDB 1HNY . Amylase IPA en m le z is an enzyme that catalysis catalyses the breakdown of starch into sugar s. Amylase is present in human saliva ..., such as rice and potato , taste slightly sweet as they are chewed because amylase turns some of their starch into sugar in the mouth. The pancreas also makes amylase alpha amylase to hydrolyse dietary ... the body with energy. Plants and some bacteria also produce amylase. As diastase , amylase was the first ...&sa X&oi book result&ct result&resnum 3&ved 0CAwQ6AEwAjgU page 296 . ref Specific amylase ... on 1,4 glycosidic bond s. Classification Amylase Main alpha Amylase The amylases EC number ... of calcium. By acting at random locations along the starch chain, amylase breaks down long ... substrate , amylase tends to be faster acting than amylase. In animal s, it is a major digestion ... at alpha Amylase . This form is also found in plants, fungi ascomycetes and basidiomycetes and bacteria Bacillus Amylase Another form of amylase, amylase EC number 3.2.1.2 alternative names 1,4 small D small glucan maltohydrolase glycogenase saccharogen amylase is also synthesized by bacteria , fungi , and plant s. Working from the non reducing end, amylase catalyzes the hydrolysis of the second ... of fruit , amylase breaks starch into maltose, resulting in the sweet flavor of ripe fruit. Both amylase and amylase are present in seeds amylase is present in an inactive form prior to germination , whereas amylase and proteases appear once germination has begun. Cereal grain amylase is key to the production of malt . Many microbe s also produce amylase to degrade extracellular starches ... more details
Image Salivary alpha amylase 1SMD.png thumb 120px Human salivary amylase calcium ion visible in pale khaki, chloride ion in green, from PDB 1SMD Image Pancreatic alpha amylase 1HNY.png thumb 120px Human pancreatic amylase Calcium ion visible in pale khaki, chloride ion in green, from PDB 1HNY Infobox protein family Symbol Alpha amylase Name Alpha amylase catalytic domain image PDB 1cyg EBI.jpg width ... family Symbol Alpha amyl C2 Name Alpha amylase C terminal beta sheet domain image PDB 1rp8 EBI.jpg width caption Crystal structure of barley alpha amylase isozyme 1 amy1 inactive mutant d180a in complex ... OPM protein CAZy CDD Infobox protein family Symbol Alpha amylase C Name Alpha amylase, C terminal ... SCOP 1ppi TCDB OPM family OPM protein CAZy CDD Amylase is an enzyme that hydrolysis hydrolyses ... page 65 ref It is the major form of amylase found in humans and other mammals. ref Voet ... found in many tissues, amylase is most prominent in pancreas pancreatic juice and saliva , each of which having its own isoform of human amylase. They behave differently on isoelectric focusing ..., all amylase isoforms link to chromosome 1p21 see AMY1A . Salivary amylase ptyalin Amylase is found in saliva and breaks starch down into maltose and dextrin . This form of amylase is also ... products. Salivary amylase is inactivated in the stomach by gastric acid . In gastric juice adjusted to pH 3.3, ptyalin was totally inactivated in 20 minutes at 37 C. In contrast, 50 of amylase activity ..., JH. Passage of salivary amylase through the stomach in humans. Digestive Diseases and Sciences 32 ... oligosaccharides protect salivary type amylase activity at acid pH. American Journal of Physiology ... least effective Genetic variation in human salivary amylase The salivary amylase gene has ... amylase, as measured by protein blot assays using antibodies to human amylase. Gene copy number ... and evolution of human amylase gene copy number variation, Nature Genetics 39 1256 1260 2007 . ref ... more details
Infobox protein family Symbol A amylase inhib Name A amylase inhib image PDB 1hoe EBI.jpg width caption crystal structure determination, refinement and the molecular model of the alpha amylase inhibitor hoe 467a Pfam PF01356 Pfam clan InterPro IPR000833 SMART PROSITE MEROPS SCOP 1hoe TCDB OPM family OPM protein CAZy CDD In molecular biology, alpha amylase inhibitor is a protein family which Enzyme inhibitor inhibits mammalia mammalian alpha amylase alpha amylases specifically, by forming a tight stoichiometric 1 1 Protein complex complex with alpha amylase. This family of enzyme inhibitor inhibitor s has no action on plant and microbe microbial alpha amylases. A crystal structure has been determined for tendamistat, the 74 amino acid inhibitor produced by Streptomyces tendae that targets a wide range of mammalian alpha amylases. ref name pmid14501112 cite journal author K nig V, V rtesy L, Schneider TR title Structure of the alpha amylase inhibitor tendamistat at 0.93 A journal Acta Crystallogr. D Biol. Crystallogr. volume 59 issue Pt 10 pages 1737 43 year 2003 month October pmid 14501112 doi 10.1107 S0907444903015828 url ref The Binding molecular binding of tendamistat to alpha amylase leads to the steric blockage of the active site of the enzyme . The crystal secondary structure structure of tendamistat revealed an immunoglobulin like protein folding fold that could potentially adopt multiple Chemical conformation conformation s. Such molecular flexibility could enable an induced fit type of binding that would both optimise binding and allow broad target Sensitivity and specificity Specificity specificity . References reflist InterPro content IPR000833 Category Protein domains ... more details
Glucosidases are glycoside hydrolase enzymes categorized under the Enzyme Commission number EC number 3.2.1. Function glucosidases are enzymes involved in breaking down complex carbohydrates such as starch and glycogen They catalyze the cleavage of individual glucosyl residues from various glycoconjugates including alpha or beta linked polymers of glucose. Members Different sources include different members in this class. Members marked with a are considered by Medical Subject Headings MeSH to be glucosidases. class wikitable Name EC Description Amylase Amylase Amylase EC number 3.2.1.1 is a digestion digestive enzyme in mammal s Amylase Amylase Amylase EC number 3.2.1.2 is a plant enzyme to break down starch Amylase Amylase Amylase EC number 3.2.1.3 is a digestive enzyme Cellulase EC number 3.2.1.4 breaks down cellulose from plant material Sucrase isomaltase EC number 3.2.1.10 Acid glucosidase EC number 3.2.1.20 is associated with Glycogen storage disease type II Beta glucosidase EC number 3.2.1.21 is associated with gaucher s disease Lactase EC number 3.2.1.23 one member of the Beta galactosidase galactosidase family, breaks down milk sugars, and its absence in adult hood causes lactose intolerance glycogen debranching enzyme Debranching enzyme EC number 3.2.1.33 Pullulanase EC number 3.2.1.41 has been used as a detergent Clinical significance They are targeted by alpha glucosidase inhibitor s such as acarbose and miglitol to control diabetes mellitus type 2 . See also DNA glycosylases Mucopolysaccharidoses External links MeshName Glucosidases Glycoside hydrolases Category Enzymes Category Hydrolases Category Carbohydrates Category EC 3.2 ... more details
Isomaltase is an enzyme that breaks the bonds linking saccharide s, which cannot be broken by amylase or maltase . It digests polysaccharides at the alpha 1 6 linkages. Its substrate, alpha limit dextrin, is a product of amylopectin digestion that retains its 1 6 linkage its alpha 1 4 linkages having already been broken down by amylase . The product of the enzymatic digestion of alpha limit dextrin by isomaltase is maltose . Isomaltase helps amylase to digest alpha limit dextrin to produce maltose. See also Sucrase isomaltase External links MeshName Isomaltase Category Hydrolases enzyme stub es Isomaltasa fr Isomaltase fi Isomaltaasi ... more details
PBB geneid 279 Pancreatic alpha amylase is an enzyme that in humans is encoded by the AMY2A gene . ref ..., Eriksson AW, Frants RR title Human pancreatic amylase is encoded by two different genes journal Nucleic ... nar 16.10.4724 ref ref name entrez cite web title Entrez Gene AMY2A amylase, alpha 2A pancreatic url ... in digestion of dietary starch and glycogen. The human genome has a cluster of several amylase genes that are expressed at high levels in either salivary gland or pancreas. This gene encodes an amylase ..., Lain J, LeBel D title Specific interactions of pancreatic amylase at acidic pH. Amylase and the major protein of the zymogen granule membrane GP 2 bind to immobilized or polymerized amylase journal ... cite journal author Groot PC, Mager WH, Henriquez NV, et al. title Evolution of the human alpha amylase ... amylase gene journal Gene volume 41 issue 2 3 pages 299 304 year 1986 pmid 2423416 doi 10.1016 0378 ... pancreatic alpha amylase gene its comparison with human salivary alpha amylase gene journal Gene volume ... Gumucio DL, Wiebauer K, Caldwell RM, et al. title Concerted evolution of human amylase genes journal ... author Samuelson LC, Wiebauer K, Gumucio DL, Meisler MH title Expression of the human amylase genes recent origin of a salivary amylase promoter from an actin pseudogene journal Nucleic Acids Res ... journal author Groot PC, Bleeker MJ, Pronk JC, et al. title The human alpha amylase multigene family ... SH, et al. title A complementary DNA sequence that predicts a human pancreatic amylase primary structure ... TB title Regional assignment of human amylase AMY to p22 p21 of chromosome 1 journal Somat. Cell ... journal author Qian M, Haser R, Buisson G, et al. title The active center of a mammalian alpha amylase. Structure of the complex of a pancreatic alpha amylase with a carbohydrate inhibitor refined ... pancreatic alpha amylase at 1.8 A resolution and comparisons with related enzymes journal Protein Sci ... amylase expressed in Pichia pastoris journal Protein Sci. volume 8 issue 3 pages 635 43 year 1999 ... more details
happens at this elevated temperature is that the alpha amylase enzyme starts to break down the starch and the viscosity thus decreases. The amount of starch break down is dependent on the alpha amylase activity and this means that the higher the activity of the alpha amylase the lower the viscosity ..., the more sprouted the grain was the higher the alpha amylase activity will be. The higher the alpha amylase activity the lower the viscosity of the slurry. The lower the viscosity of the slurry the faster ... more details
All carbohydrates absorbed in the small intestine must be hydrolyzed to monosaccharides prior to absorption. The digestion of starch begins with the action of salivary alpha amylase ptyalin, although its activity is slight in comparison with that of pancreatic amylase in the small intestine. Amylase hydrolyzes starch to alpha dextrin, which are then digested by gluco amylase alpha dextrinases to maltose and maltotriose. The products of digestion of alpha amylase and alpha dextrinase, along with dietary disaccharides are hydrolyzed to their corresponding monosaccharides by enzymes maltase, isomaltase, sucrase and lactase present in the brush border of small intestine. In the typical Western diet, digestion and absorption of carbohydrates is fast and takes place usually in the upper small intestine. However, when the diet contains carbohydrates not easily digestible, digestion and absorption take place mainly in the ileal portion of the intestine. Digestion of food continues while simplest elements are absorbed. The absorption of most digested food occurs in the small intestine through the brush border of the epithelium covering the villi small hair like structure . It is not a simple diffusion of substances, but is active and requires energy use by the epithelial cells. During the phase of carbohydrate absorption, fructose is transported by a transporter of fructose into the intestinal cell s cytosol, glucose and galactose competes with other Na transporter required for operation. From the cytosol, monosaccharides pass into the capillaries by simple or facilitated diffusion. Carbohydrates that are not digested in the small intestine, including resistant starch foods such as potatoes, beans, oats, wheat flour, as well as several non polisacac ridos oligosaccharides and starch, are digested in a variable when they reach the large intestine. The bacterial flora metabolize these compounds in the absence of oxygen. This produces gases hydrogen, carbon dioxide and methane ... more details
amylase for a wide variety of industrial as well as academic applications, e.g. ref http www.phadebas.com areas of use chemistry and research Phadebas Amylase Test Chemistry and Research Amylase activity in Detergents, Textiles and Biotech ref Alpha Amylaseamylase from detergents Biotech research & development e.g., bacterial excretion of amylase Dentistry applications Reagent for the clinical ... being that alpha amylase activity in saliva is typically several orders of magnitude higher than .... Alimentary The Phadebas Amylase test is used for determining amylase in a wide variety of food applications, for example ref http www.phadebas.com areas of use alimentary Phadebas Amylase Test Alimentary Amylase activity in Food and Beverages ref Powdered eggs Egg powder Wheat Milk powder Milk ... more details
PBB geneid 276 Alpha amylase 1 is an enzyme that in humans is encoded by the AMY1A gene . ref name entrez cite web title Entrez Gene AMY1A amylase, alpha 1A salivary url http www.ncbi.nlm.nih.gov sites ..., see Alpha Amylase . The PBB Summary template is automatically maintained by Protein Box Bot. See ... of several amylase genes that are expressed at high levels in either salivary gland or pancreas. This gene encodes an amylase isoenzyme produced by the salivary gland. Alternative splicing results in multiple ... AMY1A amylase, alpha 1A salivary url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch ... characterization of posttranslational modifications of human parotid salivary alpha amylase ... amylase multigene family through unequal, homologous, and inter and intrachromosomal crossovers. journal ... alpha amylase gene. journal Gene volume 41 issue 2 3 pages 299 304 year 1986 pmid 2423416 doi 10.1016 ... amylase expression in human pancreatic development journal Hybridoma volume 5 issue 2 pages 137 45 year ... ME title Identification of a human salivary amylase gene. Partial sequence of genomic DNA suggests ... Primary structure of human pancreatic alpha amylase gene its comparison with human salivary alpha amylase ... of human amylase genes journal Mol. Cell. Biol. volume 8 issue 3 pages 1197 205 year 1988 pmid 2452973 ... of the human amylase genes recent origin of a salivary amylase promoter from an actin pseudogene ... amylase multigene family consists of haplotypes with variable numbers of genes journal Genomics volume ... Pronk JC, Frants RR, Jansen W, et al. title Evidence of duplication of the human salivary amylase ... of human genes for amylase, proopiomelanocortin, somatostatin, and a DNA fragment D3S1 by in situ ... Regional assignment of human amylase AMY to p22 p21 of chromosome 1 journal Somat. Cell Mol. Genet ... Amylase mRNA transcripts in normal tissues and neoplasms the implication of different expressions of amylase ..., characterization, and biochemical properties of recombinant human salivary amylase journal Protein ... more details
PBB geneid 280 Alpha amylase 2B is an enzyme that in humans is encoded by the AMY2B gene . ref name pmid8268204 cite journal author Omichi K, Hase S title Identification of the characteristic amino acid sequence for human alpha amylase encoded by the AMY2B gene journal Biochim Biophys Acta volume 1203 issue 2 pages 224 9 year 1994 month Jan pmid 8268204 pmc doi ref ref name entrez cite web title Entrez Gene AMY2B amylase, alpha 2B pancreatic url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 280 accessdate ref The PBB Summary template is automatically maintained by Protein Box Bot. See Template PBB Controls to Stop updates. PBB Summary section title summary text ... genome has a cluster of several amylase genes that are expressed at high levels in either salivary gland or pancreas. This gene encodes an amylase isoenzyme produced by the pancreas. ref name entrez ... alpha amylase multigene family through unequal, homologous, and inter and intrachromosomal ... of a third type of human alpha amylase gene, AMY2B. journal Gene volume 90 issue 2 pages 281 6 ..., Caldwell RM, et al. title Concerted evolution of human amylase genes. journal Mol. Cell. Biol. volume ... K, Gumucio DL, Meisler MH title Expression of the human amylase genes recent origin of a salivary amylase promoter from an actin pseudogene. journal Nucleic Acids Res. volume 16 issue 17 pages ..., Horii A, Doi S, et al. title A novel type of human alpha amylase produced in lung carcinoid tumor. journal ... journal author Groot PC, Bleeker MJ, Pronk JC, et al. title The human alpha amylase multigene family ..., Pronk JC, et al. title Human pancreatic amylase is encoded by two different genes. journal Nucleic ... cite journal author Tricoli JV, Shows TB title Regional assignment of human amylase AMY to p22 p21 ... immunohistochemical study on amylase localization in the rat and human exocrine pancreas. journal ... author Koyama I, Komine S, Iino N, et al. title alpha Amylase expressed in human liver is encoded by the AMY ... more details
italic title Taxobox color lightgrey name Streptococcus oralis image Streptococcus oralis on Wilkins Chalgren Agar.JPG domain Bacteria phylum Firmicutes classis Bacilli ordo Lactobacillales familia Streptococcaceae genus Streptococcus species S. oralis binomial Streptococcus oralis Streptococcus oralis is a Gram positive bacterium that grows characteristically in chains. It forms small white Colony biology colonies on a Wilkins Chalgren agar plate. It is found in high numbers in the oral cavity. It has been classified as a member of the Streptococcus mitis group. Members of this group are opportunistic pathogen s. Strains of S. oralis produce neuraminidase and an IgA protease and cannot bind amylase amylase . References cite book last Marsh first Philip coauthors Michael V. Martin title Oral microbiology publisher Wright location Oxford England year 1999 pages isbn 0 7236 1051 7 Category Streptococcaceae Category Gram positive bacteria bacteria stub ar nl Streptococcus oralis es Streptococcus oralis ... more details
notability date September 2010 Sweetened potato casserole Finnish language Finnish imelletty perunalaatikko is a traditional Finnish cuisine Finnish dish from Kymenlaakso , eaten elsewhere in Finland at Christmas time ref http www.socialguide.bravehost.com cuisine.html ref . It is prepared by letting pur ed potatoes , mixed with wheat flour , stand at a temperature of around 50 C 122 F . The amylase in the flour will start to break down the potato s starches to shorter carbohydrate chains, that is sugars. The temperature cannot exceed 75 C 167 F otherwise the amylase molecules will break down ref http www.dlc.fi marianna gourmet xmas6.htm ref . It is through this process the dish gets its distinct sweet flavour, however nowadays corn syrup can be added to give it sweetness. External links http www.dlc.fi marianna gourmet gl finn.htm Glossary of Finnish dishes Sources Reflist Category Finnish cuisine Category Potato dishes Category Casserole dishes finland stub fi Imelletty perunalaatikko sv Potatisl da ... more details
Infobox protein family Symbol Alpha amylase N Name Alpha amylase, N terminal ig like domain image PDB 2d0h EBI.jpg width caption crystal structure of thermoactinomyces vulgaris r 47 alpha amylase 1 tvai mutant d356n e396q complexed with p2, a pullulan model oligosaccharide Pfam PF02903 Pfam clan InterPro IPR004185 SMART PROSITE MEROPS SCOP 1sma TCDB OPM family OPM protein CAZy CDD Infobox protein family Symbol Alpha amylase Name Alpha amylase catalytic domain image PDB 1cyg EBI.jpg width caption cyclodextrin glucanotransferase e.c.2.4.1.19 cgtase Pfam PF00128 Pfam clan CL0058 InterPro IPR006047 SMART PROSITE MEROPS SCOP 1ppi TCDB OPM family OPM protein CAZy GH13 CDD In molecular biology, glycoside hydrolase family 13 is a Protein family family of Glycoside hydrolase glycoside hydrolases . Glycoside hydrolases EC number 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non carbohydrate moiety. A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of 100 different families. ref name PUB00004870 cite journal author Henrissat B, Callebaut I, Mornon JP, Fabrega S, Lehn P, Davies G title Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases journal Proc. Natl. Acad. Sci. U.S.A. volume 92 issue 15 pages 7090 7094 year 1995 pmid 7624375 doi 10.1073 pnas.92.15.7090 pmc 41477 ref ref name PUB00005266 cite journal author Henrissat B, Davies G title Structures and mechanisms of glycosyl hydrolases journal Structure volume 3 issue 9 pages 853 859 year 1995 pmid 8535779 doi 10.1016 S0969 2126 01 00220 9 ref ref http www.expasy.ch cgi bin lists?glycosid.txt Bairoch, A. Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS PROT . 1999. ref This classification ... GH 13 of the glycosyl hydrolases. The maltogenic alpha amylase is an enzyme which catalyses hydrolysis ... more details
14 CAZY GH 14 comprises enzymes with only one known activity beta amylase EC number 3.2.1.2 . A Glu ... or the proton donor. Beta amylase ref name PUB00005234 cite journal author Fukazawa C, Mikami B, Morita Y title Primary structure and function of beta amylase journal Seikagaku volume 60 issue 3 pages ... the non reducing ends of the chains. Beta amylase is present in certain bacteria as well as in plants ... of glutamic acid 186 affinity labeled by 2,3 epoxypropyl alpha D glucopyranoside in soybean beta amylase ... H, Itoh Y, Fukazawa C, Kim CS title Residues essential for catalytic activity of soybean beta amylase ... amylase with an inhibitor alpha cyclodextrin has been determined to 3.0A resolution by X ray diffraction ... S, Morita Y title Three dimensional structure of soybean beta amylase determined at 3.0 A resolution ... more details
Italic title Taxobox color lightgrey name Bacillus amyloliquefaciens regnum Bacterium Bacteria phylum Firmicutes classis Bacilli ordo Bacillales familia Bacillaceae genus Bacillus species B. amyloliquefaciens binomial Bacillus amyloliquefaciens binomial authority Bacillus amyloliquefaciens is a species of bacterium bacteria that is the source of the BamH1 restriction enzyme . It also synthesizes a natural antibiotic protein barnase , a widely studied ribonuclease that forms a famously tight complex with its intracellular inhibitor barstar . Discovery and name B. amyloliquefaciens was discovered in soil 1943 by a Japanese scientist named Fukumoto, who gave the bacterium its name because it produced faciens a liquifying lique amylase amylo . Uses Alpha amylase from B. amyloliquefaciens is often used in starch hydrolysis. B. amyloliquefaciens is also a source of subtilisin , an enzyme that catalyzes the breakdown of proteins in a similar way to trypsin . Status as a species Between the 1940s and the 1980s, bacteriologists debated as to whether or not B. amyloliquefaciens was a separate species or a subspecies of Bacillus subtilis . The matter was settled in 1987, when a group of scientists, including Fergus G. Priest of Heriot Watt University , established it as a separate species. Full name The full name of B. amyloliquefaciens is Bacillus amyloliquefaciens sp. nov., nom. rev. The sp. nov. stands for species novum , Latin for new species , while nom. rev. is short for nomen revictum , Latin for revived name . American Type Culture Collection In the American Type Culture Collection the number for B. amyloliquefaciens is 23350 References FUKUMOTO, J. 1943. Studies on the production of bacterial amylase. I. Isolation of bacteria secreting potent amylases and their distribution in Japanese . J. Agr. Chem. Soc. Japan 19 487 503. PRIEST F.G. , GOODFELLOW M. , SHUTE L.A. and BERKELEY R.C.W. Bacillus amyloliquefaciens sp. nov., nom. rev. Int. J. Syst. Bacteriol., 1987, 37, 69 ... more details
Lintner or degrees Lintner is a unit used to measure the ability of a malt to reduce starch to sugar , that is, its mashing diastatic power . While the measurement is applicable to any amylase , in general it refers to the combined amylase and amylase used in brewing . The term is also generalized to diastatic malt extract s and separately prepared brewing enzymes. The abbreviation L is official, but in brewing applications it may conflict with L used for degrees Lovibond . JECFA, the Joint FAO WHO Expert Committee on Food Additives , defines the degree Lintner as follows A malt has a diastatic power of 100 L if 0.1 Cubic metre cc of a clear 5 infusion of the malt, acting on 100cc of a 2 starch solution at 20 C for one hour , produces sufficient reducing sugars to reduce completely 5cc of Fehling s solution . Note that the amylases used in brewing reach their peak efficiencies around 66 C. Evaluation of a malt or extract is usually done by the manufacturer rather than by the end user as a rule of thumb, the total mash ingredients grain bill of a mash should have a diastatic power of at least 40 L in order to guarantee efficient conversion of all the starches in the mash to sugars. The most active barley malts currently available have a diastatic activity of up to 160 Lintner. In Europe, diastatic activity is often stated in Windisch Kolbach unit s WK . These are related approximately to Lintner by math circ mbox Lintner frac circ mbox WK 16 3.5 math math circ mbox WK left 3.5 times circ mbox Lintner right 16 math . 100.0 Lintner equals 3.014 10 sup 7 sup katal or 18.08 enzyme unit s. External links http www.fao.org ag agn jecfa additives specs Monograph1 Additive 270.pdf Malt Carbohydrase , JECFA, 1971. Gives definitions and procedures for measuring diastatic activity. Category Brewing Category Units of catalytic activity biochem stub beer stub ... more details
Chembox Verifiedfields changed verifiedrevid 477363643 ImageFile Acarviosin.svg ImageSize 200px IUPACName Methyl 4,6 dideoxy 4 1 R ,4 S ,5 R ,6 R 4,5,6 trihydroxy 3 hydroxymethyl cyclohex 2 en 1 yl amino small D small glucopyranoside OtherNames Section1 Chembox Identifiers CASNo 80943 41 5 CASNo Ref cascite changed ?? PubChem 3083346 ChemSpiderID Ref chemspidercite correct chemspider ChemSpiderID 2340579 SMILES O C H 2 C H O C H N C H 1 C C CO C H O C H O C H 1O C H O C H 2OC C InChI 1 C14H25NO8 c1 5 8 11 19 13 21 14 22 2 23 5 15 7 3 6 4 16 9 17 12 20 10 7 18 h3,5,7 21H,4H2,1 2H3 t5 ,7 ,8 ,9 ,10 ,11 ,12 ,13 ,14 m1 s1 InChIKey KFHKERRGDZTZQJ HHHVGSORBI StdInChI Ref stdinchicite correct chemspider StdInChI 1S C14H25NO8 c1 5 8 11 19 13 21 14 22 2 23 5 15 7 3 6 4 16 9 17 12 20 10 7 18 h3,5,7 21H,4H2,1 2H3 t5 ,7 ,8 ,9 ,10 ,11 ,12 ,13 ,14 m1 s1 StdInChIKey Ref stdinchicite correct chemspider StdInChIKey KFHKERRGDZTZQJ HHHVGSORSA N Section2 Chembox Properties C 14 H 25 N 1 O 8 Appearance Density MeltingPt BoilingPt Solubility Section3 Chembox Hazards MainHazards FlashPt Autoignition Acarviosin is a sugar composed of cyclohexitol linked to a 4 amino 4,6 dideoxy small D small glucopyranose. Acarviosin is part of the potent amylase inhibitor acarbose and its derivatives. The nitrogen atom binds to amylase more tightly than the natural substrate making it more potent than other inhibitors. Several other acarviosin containing amylase inhibitors have been found in microbes including isovalertatin s ref cite pmid 11284506 ref and butytatin s ref cite pmid 11567643 ref from Streptomyces luteogriseus and longer oligosaccharide s from Streptomyces coelicoflavus . ref cite pmid 18294624 ref References Reflist Category Alpha glucosidase inhibitors Category Disaccharides Category Amino sugars Category Cyclitols ... more details
Sprout damage is undesirable germination of wheat kernels that occurs on mature, unharvested wheat when wet field conditions persist just prior to and during the harvest. Mature wheat that has been cut and left lying in the field prior to threshing is particularly vulnerable to sprout damage. Early cold weather in Canada often forces wheat producers there to cut and windrow their crop to allow for drying. Wet conditions can then cause widespread sprout damage. If it has occurred, there is a dramatic increase of the enzyme alpha amylase . The Falling Number test is a measure of the presence of this enzyme. A high falling number indicates that the wheat is sound and satisfactory for most baking processes. A low falling number indicates that harmful sprouting has occurred and is suggestive of reduced baking quality. In bread, too much alpha amylase activity will cause wet sticky bread crumb with large voids in the loaf and too little causes dry crumble bread crumb and high loaf density. References CRS article Report for Congress Agriculture A Glossary of Terms, Programs, and Laws, 2005 Edition url http ncseonline.org nle crsreports 05jun 97 905.pdf author Jasper Womach Category Wheat ... more details
Unreferenced stub auto yes date December 2009 An exoenzyme , or extracellular enzyme , is an enzyme that is secreted by a cell biology cell and that works extracellular outside of that cell . It is usually used for breaking up large molecules that would not be able to enter the cell otherwise. This term is also often used to refer to the hydrolytic digestive enzymes secreted by fungi. Examples of extracellular enzymes Amylase Angiotensin converting enzyme ACE generation of angiotensin II Lipoprotein lipase release of lipids from circulating lipoproteins Digestive enzymes breakdown of ingested nutrients Some clotting factors e.g. thrombin See also Endoenzyme Category Enzymes Enzyme stub ar de Exoenzym fr Exoenzyme pl Egzoenzymy ... more details
mergeto trypsin discuss Talk trypsin date October 2011 Trypsinogen EC 3.4.23.18 20 21 23 24 26 is the precursor form or zymogen of the pancreatic enzyme trypsin . It is found in pancreatic juice , along with amylase , lipase , and chymotrypsinogen . It is activated by enteropeptidase , which is found in the intestinal mucosa , to form trypsin . Once activated, the trypsin can activate more trypsinogen into trypsin. Trypsin cleaves the peptide bond on the carboxyl side of basic amino acid s. blood plasma Serum trypsinogen is measured using a blood test . High levels are seen in acute pancreatitis and cystic fibrosis . Functions Protein digestion . External links MeshName Trypsinogen Category EC 3.4.23 hydrolase stub ar de Trypsinogen it Tripsinogeno pl Trypsynogen pt Tripsinog nio ru sl Tripsinogen ... more details
Unreferenced date August 2009 wiktionary ase The Affix suffix ase is used in biochemistry to form names of enzyme s. The most common way to name enzymes is to add this suffix onto the end of the Substrate biochemistry substrate , e.g. an enzyme that breaks down peroxides may be called peroxidase the enzyme that produces telomere s is called telomerase . Sometimes enzymes are named for the function they perform, rather than substrate, e.g. the enzyme that polymer izes assembles DNA into strands is called polymerase see also reverse transcriptase . This suffix was likeliest extracted from the name of diastase , which was named from Greek , separation . Orgchemsuffixes See also Amylase Enzyme DNA polymerase DEFAULTSORT Ase Category Chemistry suffixes Category Biology prefixes and suffixes Category Greek suffixes ... more details
Other uses Dry disambiguation Refimprove date December 2009 Dryness is a property of alcohol ic beverage s that describes the lack of a sweet taste. This may be due to a lack of sugar s, the presence of some other taste that masks sweetness, or an underabundance of simple carbohydrate s that can be converted to sugar by enzyme s in the mouth amylase in particular . The term dry may be applied to types of beer , wine , distilled spirits , or any other form of alcoholic beverage. In a dry martini the dryness refers to the amount of vermouth used in the drink ref http www.salon.com april97 food surreal970409.html from salon.com ref . A very dry martini refers to a martini with little or no vermouth. References Reflist Bartend DEFAULTSORT Dryness Taste Category Alcoholic beverages Drink stub de Geschmacksangabe Wein fr Sec propri t de l alcool ... more details
Unreferenced stub auto yes date December 2009 Expert subject Biochemistry date February 2009 Amylolysis, or the amylolytic process, is the conversion of starch into sugar by the action of acids or enzymes like amylase . The amylolytic process is used in the brewing of alcohol from grains. Since grains contain starches but little to no simple sugars, the sugar needed to produce alcohol is derived from starch via the amylolytic process. In Brewing beer brewing , this is done through malt ing. In sake brewing, the mold Aspergillus oryzae provides amylolysis. DEFAULTSORT Amylolytic Process Category Carbohydrate chemistry Category Biochemistry Category Cooking techniques Category Japanese drinks Category Rice wine Biochemistry stub ... more details
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