OVERPRODUCTION AND SINGLE-STEP PURIFICATION OF BACILLUS-STEAROTHERMOPHILUS PEROXIDASE IN ESCHERICHIA-COLI

被引：12

作者：

LOPRASERT, S ^{[1
]}

URABE, I ^{[1
]}

OKADA, H ^{[1
]}

机构：

[1] OSAKA UNIV, FAC ENGN, DEPT FERMENTAT TECHNOL, YAMADA OKA, SUITA, OSAKA 565, JAPAN

来源：

APPLIED MICROBIOLOGY AND BIOTECHNOLOGY | 1990年 / 32卷 / 06期

关键词：

D O I：

10.1007/BF00164741

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 cloned peroxidase gene from Bacillus stearothermophilus was highly expressed in Escherichia coli. Using the high copy number plasmid which is temperature-sensitive and its own strong promoter, this thermostable peroxidase was produced at 28% of the total cell proteins when the cells were grown at 42°C. The enzyme could be easily purified from E. coli by heat treatment and single-column Sephadex G-200 chromatography. From a 200 ml culture, 30 mg of purified enzyme was obtained. The peroxidase produced by E. coli showed a thermostability, haem type and content identical with those of the peroxidase produced by B. stearothermophilus. © 1990 Springer-Verlag.

引用

页码：690 / 692

页数：3

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