CLEAVAGE OF BACILLUS-SUBTILIS ENDO-BETA-1,4-GLUCANASE BY B-MEGATERIUM PROTEASE

被引：9

作者：

AHN, DH

KIM, H

PACK, MY

机构：

[1] SUNCHON NATL UNIV,DEPT AGR CHEM,SUNCHON 540742,SOUTH KOREA

[2] KAIST,DEPT BIOTECHNOL,TAEJON 305338,SOUTH KOREA

来源：

BIOTECHNOLOGY LETTERS | 1993年 / 15卷 / 02期

关键词：

D O I：

10.1007/BF00133011

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：

A protease secreted by B. megaterium ATCC 14945 was purified by ammonium sulfate fractionation, Q-Sepharose, Sephadex G-75, and hydroxyapatite chromatography and its molecular weight was estimated to be 38 kD. The purified protease caused the cleavage of 52 kD B. subtilis endo-beta-1,4-glucanase expressed in B. megaterium. The enzyme was most active at pH 7.5 and 55-degrees-C. Calcium ion was required for the enzyme activity and the activity was almost completely inhibited by EDTA. The protease was not inhibited by phenylmethylsulfonyl fluoride.

引用

页码：127 / 132

页数：6

共 21 条

[11]

LOWRY OH, 1951, J BIOL CHEM, V193, P265

[12]

MEZES PSF, 1985, MOL BIOL BACILLI, V2, P151

[13] BIOCHEMICAL AND PHYSIOLOGICAL PROPERTIES OF AN EXTRACELLULAR PROTEASE PRODUCED BY BACILLUS-MEGATERIUM [J].