推荐产品
生物来源
hog pancreas
表单
powder
比活
~50 U/mg
储存温度
−20°C
一般描述
胰α淀粉酶由胰腺泡细胞产生并释放至十二指肠。它是胰液的主要分子。[1]
生化/生理作用
单位定义
1单位酶相当于在pH 6.9和25℃条件下,每分钟释放1 μmol麦芽糖所需的酶量(淀粉符合Zulkowsky,货号85642,作为底物)
警示用语:
Danger
危险声明
预防措施声明
危险分类
Resp. Sens. 1
储存分类代码
11 - Combustible Solids
WGK
WGK 1
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
其他客户在看
Muhammad H Alu'datt et al.
Food chemistry, 240, 784-798 (2017-09-28)
This investigation was performed to assess the effects of sonication on the structure of protein, extractability of phenolics, and biological properties of isolated proteins and protein co-precipitates prepared from brewers' spent grain and soybean flour. Scanning electron micrographs revealed that
Paula Monteiro de Souza et al.
Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology], 41(4), 850-861 (2010-10-01)
Amylases are one of the main enzymes used in industry. Such enzymes hydrolyze the starch molecules into polymers composed of glucose units. Amylases have potential application in a wide number of industrial processes such as food, fermentation and pharmaceutical industries.
I. Kluh
Collection of Czechoslovak Chemical Communications, 44, 288-288 (1979)
Yufang Liu et al.
Journal of agricultural and food chemistry, 65(9), 1865-1873 (2017-02-15)
Health-promoting effects of kefir may be partially caused by bioactive peptides. To evaluate their formation or degradation during gastrointestinal digestion, we monitored changes of the peptide profile in a model of (1) oral, (2) gastric, and (3) small intestinal digestion
Mechanistic study on inhibition of porcine pancreatic α-amylase using the flavonoids from dandelion.
Yanmei Huang et al.
Food chemistry, 344, 128610-128610 (2020-11-23)
This study was designed to investigate quantitatively the inhibition and molecular mechanism of pancreatic α-amylase exhibited by flavonoids from dandelion to reveal its potential use in relieving postprandial hyperglycemia. The results show that the flavonoids reversibly inhibited the α-amylase in
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