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 . Amylase is present in human saliva , where ..., 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 EC number 3.2.1.1 CAS registry ... of calcium. By acting at random locations along the starch chain, amylase breaks down long chain ... substrate , amylase tends to be faster acting than amylase. In animal s, it is a major digestion ... Amylase . Also found in plants adequately , fungi ascomycetes and basidiomycetes and bacteria Bacillus Amylase EC number 3.2.1.2 alternate names 1,4 small D small glucan maltohydrolase glycogenase saccharogen amylase Another form of amylase, amylase is also synthesized by bacteria , fungi , and plant s. Working from the non reducing end, amylase catalyzes the hydrolysis of the second ... , 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. Animal ... 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 . Amylase ... Baltimore , Maryland, USA isbn 978068340007690000 page 65 ref It is the major form of amylase ... by many fungi. In human physiology Although 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 ... monoclonal antibody monoclonal antibodies . In humans, 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 called ptyalin IPA en ta l n . ref Ptyalin was named by Swedish ... an enzyme that acts on branched products. Salivary amylase is inactivated in the stomach by gastric ... sup 0 sup C. In contrast, 50 of amylase activity remained after 150 minutes of exposure to gastric juice at pH 4.3. ref Fried, M, Abramson, S, Meyer, JH. Passage of salivary amylase through the stomach ... Rosenblum, JL, Irwin, CI, Alpers, DH. Starch and glucose oligosaccharides protect salivary type amylase ... ptyalin salivary amylase The salivary amylase gene has undergone duplication during evolution, and DNA ... of gene copies correlates with the levels of salivary amylase, as measured by protein blot assays using antibodies to human amylase. Gene copy number is associated with apparent evolutionary exposure to high starch diets. ref Perry, GH, et al. Diet and evolution of human amylase gene copy ... copies of the amylase gene one allele with 10 copies, and a second allele with 4 copies . The Japanese ... of the salivary amylase gene may have enhanced survival coincident to a shift to a starchy diet during human evolution. Pancreatic amylase Pancreatic amylase randomly cleaves the glycosidic bond 1 ... 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 amylose 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
Glucosidases are glycoside hydrolase enzymes categorized under the 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 adulthood 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
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 isoenzyme produced by the pancreas. ref name entrez cite web title Entrez Gene AMY2A amylase, alpha ... 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 Biochem. Cell Biol. volume 70 issue ... WH, Henriquez NV, et al. title Evolution of the human alpha amylase multigene family through unequal ... Y, Emi M, et al. title Primary structure of human salivary alpha amylase gene. journal Gene volume ... Horii A, Emi M, Tomita N, et al. title Primary structure of human pancreatic alpha amylase gene its comparison with human salivary alpha amylase gene. journal Gene volume 60 issue 1 pages 57 64 year ... 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 8261 ... MJ, Pronk JC, et al. title The human alpha amylase multigene family consists of haplotypes with variable ... DNA sequence that predicts a human pancreatic amylase primary structure consistent with the electrophoretic ... of human amylase AMY to p22 p21 of chromosome 1. journal Somat. Cell Mol. Genet. volume 10 issue ..., 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 to 2.2 A resolution. journal ... more details
unreferenced date June 2010 Orphan date June 2010 Merge Carbohydrate catabolism date June 2010 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, although their activity is slight in comparison with that made by 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. Continue the digestion of food while their simplest elements are absorbed. The absorption of most of digested food occurs in the small intestine through the brush border of the epithelium covering the villi. It is not a simple diffusion of substances, but is active and requires energy use by the epithelial cells In a phase of carbohydrate absorption, fructose is transported by a transporter of fructose into the intestinal cell cytosol, glucose and galactose competes with other Na transporter required for operation. The cytosol, monosaccharides pass into the capillaries by simple diffusion 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 a ... 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 ... 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 gene. journal Gene volume 60 issue 1 pages 57 64 year 1988 pmid 2450054 doi 10.1016 0378 1119 ... 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 ... alpha amylase multigene family consists of haplotypes with variable numbers of genes. journal Genomics ... amylase gene. journal Hum. Genet. volume 60 issue 1 pages 32 5 year 1982 pmid 6176528 doi 10.1007 BF00281260 ... localization of human genes for amylase, proopiomelanocortin, somatostatin, and a DNA fragment ... TB title Regional assignment of human amylase AMY to p22 p21 of chromosome 1. journal Somat. Cell Mol ... al. title Amylase mRNA transcripts in normal tissues and neoplasms the implication of different expressions ... 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
determining amylase for a wide variety of industrial as well as academic applications, e.g. ref http www.phadebas.com applications research quality 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 ... 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
Descri o do arquivo Cope & Lyra model of pleural needle for biopsy of the pleura on exudative pleural effusions. Once identified as exudative, additional evaluation is needed to determine the cause of the excess fluid, and pleural fluid amylase, glucose, pH and cell counts are obtained. The fluid is also sent for Gram staining and culture, and, if suspicious for tuberculosis, examination for TB markers adenosine deaminase 45 IU L, interferon gamma 140 pg mL, or positive polymerase chain reaction PCR for tuberculous DNA . Pleural fluid amylase is elevated in cases of esophageal rupture, Pancreatic fistula pancreatic pleural effusion , or cancer. Glucose is decreased with cancer, bacterial infections, or rheumatoid pleuritis . Pleural fluid pH is low in empyema 7.2 and may be low in cancer. If cancer is suspected, the pleural fluid is sent for cytology. If cytology is negative, and cancer is still suspected, either a thoracoscopy , or needle biopsy of the pleura may be performed. Reference http www.chestjournal.org content 112 1 296.2.full.pdf Licensing PD self date May 2009 ... 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 numbers 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
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
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 peptide bond on 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 hydrolase stub category EC 3.4.23 ar de Trypsinogen pl Trypsynogen pt Tripsinog nio ru sl Tripsinogen ... 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 Organic chemistry Category Biochemistry Category Cooking techniques Category Japanese drinks Category Rice wine Biochemistry stub ... 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 71. ... 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
Unreferenced stub auto yes date December 2009 Drugbox IUPAC name image synonyms CAS number CAS supplemental ATC prefix A09 ATC suffix AA02 ATC supplemental PubChem DrugBank KEGG chemical formula molecular weight smiles bioavailability protein bound metabolism elimination half life excretion pregnancy AU A B1 B2 B3 C D X pregnancy US A B C D X pregnancy category legal AU S2, S3, S4, S5, S6, S7, S8, S9 or Unscheduled legal CA Schedule I, II, III, IV, V, VI, VII, VIII legal UK GSL, P, POM, CD, or Class A, B, C legal US OTC Rx only Schedule I, II, III, IV, V legal status routes of administration Oral Pancreatin trade names PANSTAL Cipla Supracare , Zenpep Eurand , Creon Abbott , Nutrizym Merck , Pancrease HL Janssen Cilag and Pancrex Paines & Byrne is a mixture of several digestive enzyme s produced by the Exocrine gland exocrine cells of the pancreas . It is composed of amylase , lipase and protease . This mixture is used to treat conditions in which pancreas pancreatic secretions are deficient, such as pancreatectomy surgical pancreatectomy , pancreatitis and cystic fibrosis . It has been claimed to help with food allergies, celiac disease, autoimmune disease, cancer and weight loss. Pancreatin is sometimes called pancreatic acid , although it is neither a single chemical substance nor an acid. Pancreatin contains the pancreatic enzymes trypsin , amylase and lipase. A similar mixture of enzymes is sold as pancrelipase , which contains more active lipase enzyme than does pancreatin. The trypsin found in pancreatin works to hydrolyze proteins into oligopeptides amylase hydrolyzes starches into oligosaccharides and the disaccharide maltose and lipase hydrolyzes triglycerides into fatty acids and glycerols. Pancreatin is an effective enzyme supplement for replacing missing pancreatic enzymes, and aids in the digestion of foods in cases of pancreatic insufficiency. Some contact lens cleaning solutions contain Pig porcine pancreatin extractives to assist in the intended pro ... 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
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
Multiple issues orphan February 2010 notability February 2010 unreferenced February 2010 American Health Inc. is a company that manufactures health supplements. It is located in Holbrook, New York . One of its products is labeled the Chewable Original Papaya Enzyme with the attached registered trademark, The After Meal dietary supplement Supplement . Each three tablet serving contains 45 mg papain , 6 mg amylase , 6 mg protease , and 3 mg papaya fruit Carica papaya . Each tablet is white, ovular and oblong, and of the dimensions 10mm by 5mm by 3mm and slightly sweet . External links http nnfa.org Natural Products Association Dead link date February 2010 Category Manufacturing companies based in New York Category Companies based in Suffolk County, New York US manufacturing company stub ... more details
Image CGTase domains.jpg thumb 200px CGTase ribbon diagram Cyclodextrin glycosyl transferase also Cyclodextrin glucosyltransferase or Cyclodextrin glucanotransferase or CGTase for short EC number 2.4.1.19 is a Bacterium bacterial enzyme belonging to the same family of the amylase amylase specifically known as glycosyl hydrolase family 13. This peculiar enzyme is capable of catalyzing more than one reaction with the most important being the synthesis of non reducing cyclic dextrin s known as cyclodextrin s starting from starch , amylose , and other polysaccharide s. CGTase is an enzyme common to many bacterial species, in particular of the Bacillus genus e.g. B. circulans , B. macerans and B. stearothermophilus , as well as to some archaea , but it is not known to be present in any other species. Catalytic activities All of the CGTases can catalyze up to four reactions cyclization, coupling, disproportionation and hydrolysis. All these activities share the same catalytic mechanism which is common to all glycosyl hydrolases. Cyclization is the process through which a linear polysaccharidic chain is cleaved and the two ends of the cleaved fragment are joined to produce a circular dextrin cyclodextrin or CD on the basis of the number of sugar residues this circular product is made of three main type of cyclodextrins can be distinguished, CD with six residues, CD with seven residues and CD with eight residues. The coupling reaction can be easily described as the reverse process of cyclization the enzyme cleaves a cyclodextrin to produce a linear dextrin which is subsequently joined to a linear oligosaccharide. Disproportionation is very similar to coupling, but the cleaved dextrin is not a cyclodextrin, but a linear oligosaccharide that is then joined to a second oligosaccharide. CGTase also has a weak hydrolyzing activity which consists in cleaving the longer polysaccharidic chains into shorter fragments. References Biwer A, Antranikian G, Heinzle E. Enzymatic p ... more details
In physiology , the term serous fluid is used for various bodily fluid s that are typically pale yellow and transparent, and of a benign nature, that fill the inside of body cavity body cavities . Serous fluid originates from serous gland s, with secretions enriched with protein s and water. Serous fluid may also originate from mixed glands, which contain both mucous and serous cells. A common trait of serous fluids is their role in assisting digestion , excretion , and Respiratory system respiration . In medical fields, especially cytopathology , serous fluid is a synonym for effusion fluid s from various body cavities . There are many causes of effusions which include involvement of the cavity by cancer . Cytopathology evaluation is recommended to evaluate the causes of effusions in these cavities. ref name Shidham Examples Saliva consists of mucus and serous fluid the serous fluid contains the enzyme amylase important for the digestion of carbohydrate s. Minor Von Ebner s glands salivary glands of von Ebner present on the tongue secretion secrete the amylase. The parotid gland produces purely serous saliva. The other major salivary gland s produce mixed serous and mucus saliva. Another type of serous fluid is secreted by the serous membrane s or serosa , two layered membranes which line the body cavities . The serous fluid between the two layers acts as a lubricant and reduces friction from muscle movement. Cytopathologic evaluation is recommended to evaluate the causes of fluid accumulation which include involvement of the cavity by cancer. ref name Shidham cite book author Vinod B. Shidham & Barbara F. Atkinson title Cytopathologic Diagnosis of Serous Fluids publisher Elsevier year 2007 isbn 9781416001454 ref Blood serum is the liquid part of blood remaining after coagulation clotting , and is therefore lacking in clotting factors and distinct from blood plasma . See also Blood plasma , the liquid portion of blood with clotting factor s Seroma , a pocket of ser ... more details
taxobox name Chaerophyllum bulbosum image Koeh 177.jpg regnum Plantae unranked divisio Angiosperms unranked classis Eudicots unranked ordo Asterids ordo Apiales familia Apiaceae genus Chaerophyllum species C. bulbosum binomial Chaerophyllum bulbosum binomial authority Carolus Linnaeus L. synonyms Chaerophyllum prescottii Chaerophyllum bulbosum is a species of flowering plant in the Apiaceae carrot family known by several common names, including turnip rooted chervil , tuberous rooted chervil , bulbous chervil , and parsnip chervil . It is native to Europe and Western Asia . This is a tall annual herb with fringelike divided leaves and large umbel s of white flowers. The plant is cultivated on a small scale in parts of Europe for the edible root, which looks like a dark gray carrot with yellowish white flesh. After harvest it is stored for a few months, during which time the sugar content increases via hydrolysis of starch by amylase s. ref Geoffriau, E., et al. 2005 . Evolution of amylase activity in tuberous rooted chervil Chaerophyllum bulbosum L. roots during storage at various temperatures. Acta Horticulturae 3 682. ref Storage also allows the development of the root s flavor, which is reminiscent of chestnut . The root is prepared by boiling. References reflist External links http www.hort.purdue.edu newcrop proceedings1990 V1 422.html C. bulbosum as a New Crop http www.guenther blaich.de pflseite.php?par Chaerophyllum bulbosum&abs pflti&fm Photo gallery Edible Apiaceae Category Edible Apiaceae Category Flora of Western Asia Category Flora of Europe Category Root vegetables Apiaceae stub vegetable stub de Knolliger K lberkropf es Chaerophyllum bulbosum fr Cerfeuil tub reux nl Knolribzaad ro Baraboi plant ru sv Rotk rvel ... more details
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