PARTIAL-PURIFICATION AND CHARACTERIZATION OF AMINOPEPTIDASES FROM DEBITTERING AND NONDEBITTERING STRAINS OF LACTOBACILLUS-CASEI

被引:0
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作者
ELABBOUDI, M
ELSODA, M
PANDIAN, S
SIMARD, RE
OLSON, N
机构
[1] UNIV ALEXANDRIA,ALEXANDRIA,EGYPT
[2] UNIV WISCONSIN,CTR DAIRY RES,MADISON,WI 53706
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中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
Partial purification and characterization of aminopeptidase from debittering and non-debittering strains of Lactobacillus casei ssp. were undertaken. The aminopeptidase activity of both strains was optimal at pH 7.0 and at 40-degrees-C. The enzymes were strongly inactivated by EDTA and 1:10 phenanthroline and activated by bivalent cations Co++ and Mg++. The aminopeptidase of a debittering strain showed a much broader substrate specificity when compared to the non-debittering strain.
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页码:366 / 370
页数:5
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