Characterization and chillproofing activity of two enzymes from Streptomyces species

被引:2
作者
Etok, CA [1 ]
Eka, OU [1 ]
机构
[1] UNIV CALABAR,DEPT BIOCHEM,CALABAR,NIGERIA
关键词
D O I
10.1002/jobm.3620360204
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Two enzymes, amylase and protease of Streptomyces species were purified by a combination of ion exchange chromatography and gel filtration and characterized. The amylase had an exoaction on starch yielding maltose as a major end product and was identified as beta-amylase. The purified amylase had a molecular weight of 48,000 and was maximally active at 35 degrees C and at pH 6.0. On the other hand, protease had a molecular weight of 21,000 and was most active at pH 10.0 and at a temperature of 30 degrees C. The K-m or MICHAELIS constant of amylase for maize starch was 0.333 mg/ml while that of protease for casein was 2.5 mg/ml. The feasibility of using the purified protease for various industrial application especially in the chillproofing of beer is discussed.
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页码:83 / 88
页数:6
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