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Another form of amylase, β-amylase (EC 3.2.1.2 ) (alternative names: 1,4-α-D-glucan maltohydrolase; glycogenase; saccharogen amylase) is also synthesized by bacteria, fungi, and plants. Working from the non-reducing end, β-amylase catalyzes the hydrolysis of the second α-1,4 glycosidic bond, cleaving off two glucose units at a
β-Amylase (EC 3.2.1.2, saccharogen amylase, glycogenase) is an enzyme with the systematic name 4-α-D-glucan maltohydrolase. [ 2 ] [ 3 ] [ 4 ] It catalyses the following reaction: Hydrolysis of (1→4)-α- D -glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
In biochemistry, lipase (/ ˈ l aɪ p eɪ s, ˈ l aɪ p eɪ z / LY-payss, LY-payz) refers to a class of enzymes that catalyzes the hydrolysis of fats. Some lipases display broad substrate scope including esters of cholesterol , phospholipids , and of lipid-soluble vitamins [ 1 ] [ 2 ] and sphingomyelinases ; [ 3 ] however, these are usually ...
The first step in the production of high-fructose corn syrup is the treatment of cornstarch with α-amylase, which cleaves the long starch polymers into shorter chains of oligosaccharides. An α-amylase called "Termamyl", sourced from Bacillus licheniformis, is also used in some detergents, especially dishwashing and starch-removing detergents ...
The optimal growing conditions of this organism is in a facultative anaerobic environment with an average temperature of about 40 °C. The Becton/Dickinson BBL Enterotube II system for identification of members of the order Enterobacterales inoculated with P. vulgaris may yield the following results:
Studies have shown that even in these cases, lingual lipase is present in normal amounts, [5] and contributes to greater than 90% of total lipase activity in duodenum. [2] This can be attributed to the fact that lingual lipase has a low pH optimum and can thus remain active through the stomach into the duodenum, where there is a low pH in ...
Optimum pH pH description Pepsin 1.5–1.6 Highly acidic Invertase 4.5 Acidic Lipase (stomach) 4.0–5.0 Acidic Lipase (castor oil) 4.7 Acidic Lipase (pancreas) 8.0 Alkaline Amylase (malt) 4.6–5.2 Acidic Amylase (pancreas) 6.7–7.0 Acidic-neutral Cellobiase 5.0 Acidic Maltase 6.1–6.8 Acidic Sucrase 6.2 Acidic Catalase 7.0 Neutral Urease 7.0
The production of a particular digestive exoenzyme by a bacterial cell can be assessed using plate assays. Bacteria are streaked across the agar, and are left to incubate. The release of the enzyme into the surroundings of the cell cause the breakdown of the macromolecule on the plate. If a reaction does not occur, this means that the bacteria ...