生物来源
Bacillus licheniformis
质量水平
形式
liquid
比活
≥0.75 Anson units/mL
制造商/商品名称
Calbiochem®
储存条件
OK to freeze
技术
activity assay: suitable
颜色
dark brown
应用
life science and biopharma
运输
ambient
储存温度
2-8°C
一般描述
Alcalase® is a serine endopeptidase that consists primarily of subtilisin A.
应用
Alcalase® Enzyme, Bacillus licheniformis has been used in the proteolytic digestion and extraction of polysaccharides in various sponge species. It has also been used as an endoprotease enzyme in enzymatic hydrolysis for the production of fish protein hydrolysate.
生化/生理作用
Alcalase® is suitable for the hydrolysis of proteins with an optimal pH of 7.0-8.5. It is used as an additive in detergent, dehairing, and bating leather. Alcalase is also used in meat tenderizing, cheese flavor development, baked manufacture, and improving the digestibility of animal feeds. Commercial Alcalase® comprises a liquid enzymatic preparation containing 50% glycerol, 41% water, and 9% protease extract from Bacillus licheniformis.
警告
Toxicity: Harmful (C)
单位定义
One unit is defined as the amount of enzyme that will release 1.0 µmol L-tyrosine from hemoglobin per min at 25°C, pH 7.5.
重悬
Please refer to the vial label for lot-specific density.
法律信息
Alcalase is a registered trademark of Novozymes Corp.
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
警示用语：
Danger
危险声明
危险分类
Aquatic Chronic 3 - Eye Dam. 1 - Resp. Sens. 1
WGK
WGK 2
闪点(°F)
Not applicable
闪点(°C)
Not applicable
法规信息
监管及禁止进口产品
Monitoring of sulfated polysaccharide content in marine sponges by Raman spectroscopy
Maia LF, et al.
Vibrational Spectroscopy, 87, 149-156 (2016)
Veymar G Tacias-Pascacio et al.
International journal of biological macromolecules, 165(Pt B), 2143-2196 (2020-10-23)
This review aims to cover the uses of the commercially available protease Alcalase in the production of biologically active peptides since 2010. Immobilization of Alcalase has also been reviewed, as immobilization of the enzyme may improve the final reaction design
Fish protein hydrolysate production by acid and enzymatic hydrolysis
Wisuthiphaet N, et al.
Applied Science and Engineering Progress, 9(4) (2016)
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