Alpha Amylase

• CAS No.: 9000-90-2
• Color: White
• Appearance: Powder
• Transport Package: Paper
• Specification: large
• Trademark: china
• Model NO.: E1422
• Origin: China
• HS Code: 2930400000
• Production Capacity: 5000kg/Year

Product Description

English name: α -Amylase (Bacilus subtilis); 1,4- α -D-Glucan-glucanohydrolase Other names: medium temperature amylase; liquefied amylase; liquefied ase; α -1,4 dextrase; bacterial amylase; α -amylase; dextrinase [2] CAS number: 9000-90-2 Level: BioChemika Vitality: 50U / mg Definition of vitality: 1 U corresponds to the amount of enzyme which liberates 1 μmole maltose per minute at pH 6.9 at 25 °C (starch acc. to Zulkowsky, Catalog No.85642, as substrate). Character: yellow-brown or white-like powder. Extracted from B. subtilis Use: Biochemical studies. Can make the rapid liquefaction of starch to produce low molecules. [3] Save: 2~8ºC property broadcast edit The heat resistance of α -amylase is very strong, and in the presence of moderate calcium salt and table salt, the pH value of 5.3 to 7.0 still keeps the activity from 93 to 95ºC. In order to facilitate the preservation, the appropriate amount of calcium carbonate is often added as an anti-knot agent to prevent agglomeration. α-Amylase can hydrolyze the α -1,4-glycosidic bond inside starch, and the hydrolyzed products are dextrins, oligosaccharides and monosaccharides. After the enzyme action, the viscosity of gelatinized starch can be rapidly reduced and become liquefied starch, so it is also known as liquefied amylase, liquefied enzyme, α -1,4-dextrase. α-When amylase takes amylose as the substrate, the reaction is generally carried out in two stages. First, amylose degrades rapidly, producing oligosaccharides. At this stage, the viscosity of amylose and its ability to react with iodine are rapidly decreased. The reaction in the second phase is much slower than that in the first phase, including the slow hydrolysis of the oligosaccharides to produce the final products of glucose and maltose. α-Amylase acting on branch starch produces glucose, maltose, and a series of limiting dextrins (oligosaccharides consisting of four or more glucose groups), all of which contain α -1,6-glycosidic bonds. The α-amylase molecule contains a fairly firmly bound calcium ion, which is not directly involved in the formation of the enzyme-substrate complex, and functions to maintain the structure of the enzyme with the maximum stability and the highest activity. α-The optimal pH ranged between 4.5 and 7.0, and the optimal pH-values of α -amylase from human saliva and pig pancreas ranged from 6.0 to 7.0; the optimal pH of B. subtilis α -amylase ranged from 5.0 to 7.0; the optimal pH of B pothermophilus-amylase was about 3.0; the optimal pH of α -amylase from sorghum shoots was 4.8 to 5.4; and the optimal pH of wheat α -amylase was about 4.5, the activity decreased after 5. According to the thermostability of α -amylase can be divided into thermostable α -amylase and mesophile-amylase. In thermostable α -amylase, enzyme preparations produced by Bacillus starch liquefied and Bacillus licheniformis have been widely used in food processing. The temperature has different effects on the vitality of these two enzymes, bacillus licheniformis-amylase optimum temperature is 92ºC, while the optimal temperature of Bacillus starch-amylase is only 70ºC, Except for the difference in thermal stability, the end products of the two enzymes acting on starch is not the same [1]. function broadcast edit Hydrolyze only the α -1,4-glucosidic bond in the starch molecular chain, and cut the starch chain into short-chain dextrins, oligosaccharides and a small amount of maltose and glucose, so that the starch viscosity rapidly decreased to achieve the purpose of "liquefaction" [4]. Toxicological basis broadcast edit (1) LD50 mice were orally administered at 7,375 mg / kg. (2) ADI: Acceptable [from Aspergillus oryzae (JECFA, 1987)]; not required [from Bacillus subtilis, Bacillus thermothermophilus (JECFA, 1990) and Bacillus licheniformis (JECFA, 2003)]. (3) The mutagenic effect. This product has no obvious accumulation effect in the body, and no mutagenic effect of [4]. apply broadcast edit α -Amylase is mainly used for hydrolyzing starch to make caramel, glucose and syrup, as well as the production of dextrin, beer, yellow rice wine, alcohol, soy sauce, vinegar, fruit juice and monosodium glutamate. It is also used in the production of bread to improve the dough, such as reducing the dough viscosity, accelerating the fermentation process, increasing the sugar content and alleviating the aging of the bread. In infant food for cereal material pretreatment. In addition, it is also used in vegetable processing. Amount: in subtilis α -amylase (6000 IU / g), the added amount is about 0.1% [3].