PURIFICATION AND PROPERTIES OF ALPHA-AMYLASE FROM MICROCOCCUS-VARIANS

被引：3

作者：

ADELEYE, AI ^{[1
]}

机构：

[1] OBAFEMI AWOLOWO UNIV,DEPT MICROBIOL,IFE,NIGERIA

来源：

JOURNAL OF BASIC MICROBIOLOGY | 1990年 / 30卷 / 10期

关键词：

D O I：

10.1002/jobm.3620301003

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

An extracellular alpha-amylase from Micrococcus varians was partially purified (63 fold) by ammonium sulphate precipitation followed by dialysis and separated by molecular exclusion into three components with molecular weights ranging from approximately 14,000 to 56,000. The amylase had a pH optimum of 7.0 and apparent Km of approximately 0.5 mg ml-1 for starch. The enzyme activity was stimulated by Ca2+ and Mg2+ ions. Optimum temperature was 45 C while there was a complete absence of activity at 70 C in 20 min. Ethylene diaminetetra acetic acid (EDTA) and iodoacetic acid (IA) inhibited the activity of the enzyme.

引用

页码：717 / 722

页数：6

共 16 条

[1] PRODUCTION AND CONTROL OF EXTRACELLULAR ALPHA-AMYLASE IN MICROCOCCUS-VARIANS [J].