期刊
JOURNAL OF AQUATIC FOOD PRODUCT TECHNOLOGY
卷 29, 期 4, 页码 322-334出版社
TAYLOR & FRANCIS INC
DOI: 10.1080/10498850.2020.1733157
关键词
Trypsin; chymotrypsin; pancreatic lipase; enzymatic activity; Totoaba macdonaldi
资金
- Biological and Health Sciences Division of the University of Sonora, Hermosillo, Sonora, Mexico [USO313003465]
Molecular weights of trypsin, chymotrypsin, and lipase from anterior intestine and pyloric caeca of Totoaba macdonaldi were evaluated, as well as optimum temperature and pH for activity of the proteases. Trypsin was 24.1 kDa and effectively hydrolyzed N alpha-benzoyl-DL-arginine 4-nitroanilide hydrochloride at optimum pH and temperature of 8 and 65 degrees C, respectively. Chymotrypsin was 25.9 kDa and showed higher hydrolytic activity for N-benzoyl-L-tyrosine ethyl ester at pH 8 and 45 degrees C, with a wider range of statistically similar activity values. Two pancreatic lipases of 70.2 and 47.5 kDa were detected, which could be the uncleaved and the final form of a colipase-dependent pancreatic lipase, since enzyme activity was detected without supplementation of bile salts and supplementing them inhibited activity.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据