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PURIFICATION AND CHARACTERIZATION OF LACTOBACILLUS-LACTIS BETA-D-GALACTOSIDASE FROM ESCHERICHIA-COLI-CELLS
被引：0
作者：
SAMEK, Z
TURNA, J
GRONES, J
机构：
来源：
关键词：
BETA-D-GALACTOSIDASE PURIFICATION;
KM CONSTANT;
PH OPTIMUM;
TEMPERATURE OPTIMUM;
BETA-D-GALACTOSIDASE STABILITY;
LACTOBACILLUS-LACTIS;
447;
D O I：
暂无
中图分类号：
Q [生物科学];
学科分类号：
07 ;
0710 ;
09 ;
摘要：
Beta-D-galactosidase from Lactobacillus lactis 447 derived from recombinant E. coli MC 4100 was purified and characterized. Physico-chemical properties of the enzyme were compared with those of beta-D-galactosidases from a naturally occuring L. lactis 447 and a overproducing E. coli strain. 10.8-fold purification of the enzyme was achieved following its isolation. The Michaelis constant for beta-D-galactosidase was found to be 1.69 x 10(-4) mol. l(-1), optimum pH was about pH 7 and optimum temperature ranged from 50-degrees-C to 54-degrees-C. The enzyme proved to be thermally stable at 50-degrees-C.
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页码：1089 / 1095
页数：7
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