PURIFICATION AND PROPERTIES OF AN ENDOGLUCANASE FROM A BACILLUS ISOLATE

被引：21

作者：

SHARMA, P ^{[1
]}

GUPTA, JK ^{[1
]}

VADEHRA, DV ^{[1
]}

DUBE, DK ^{[1
]}

机构：

[1] CSIR,INST MICROBIAL TECHNOL,CHANDIGARH,INDIA

来源：

ENZYME AND MICROBIAL TECHNOLOGY | 1990年 / 12卷 / 02期

关键词：

Bacillus sp. PDV; CMC; Endoglucanase (E.C. 3.2.1.4); enzyme purification; stability; substrate specificity;

D O I：

10.1016/0141-0229(90)90087-7

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

The thermophilic soil isolate, Bacillus sp. PDV, produced endoglucanase when grown on glucose and could not utilize carboxymethyl cellulose (CMC) or Avicel as growth substrates. The CMCase was purified on a DEAE-Sephacel ion exchange column followed by Biogel-A-0.5m and Superose-6 gel filtration columns. The purified CMCase was found to be homogeneous on polyacrylamide gel electrophoresis with silver staining and had a molecular weight of 33,000 (SDS-PAGE and Sephadex G-100 gel filtration). It showed activity towards crystalline forms of cellulose such as cotton and Avicel and was stable in the pH range of 4-10 and temperature up to 60°C. The enzyme hydrolysed CMC with pH and temperature optima of 5.0 and 60°C and a Km of 0.588 mg ml-1. The enzyme activity was completely inhibited by Hg2+, while other metalions, chelators, various oxidizing agents, and repeated freezing and thawing had no marked effect on activity. Reducing agents, in general, increased the activity. © 1990.

引用

页码：132 / 137

页数：6

共 25 条

[1] GEL-FILTRATION BEHAVIOUR OF PROTEINS RELATED TO THEIR MOLECULAR WEIGHTS OVER A WIDE RANGE [J].