PURIFICATION AND SOME PROPERTIES OF CHITINASES FROM AEROMONAS SP NO-10S-24

被引：57

作者：

UEDA, M

ARAI, M

机构：

[1] Department of Agricultural Chemistry, College of Agriculture, University of Osaka Prefecture, Sakai

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 1992年 / 56卷 / 03期

关键词：

D O I：

10.1271/bbb.56.460

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Chitinases I and II were purified from the culture supernant of Aeromonas sp. 10S-24 by ammonium sulfate precipitation, SP-Sephadex C-50 chromatography, Sephacryl S-200 gel filtration, and chromatofocusing. Both enzymes were most active at pH 4.0 and the optimum temperature for I and II were 50-degrees-C and 60-degrees-C. Chitinase I was stable at pHs between 4 and 9 and at temperatures below 50-degrees-C and chitinase II was stable at pHs between 5 and 7 and at temperatures below 45-degrees-C. The molecular weights were estimated by SDS polyacrylamide gel electrophoresis to be 112,000 and 115,000 for I and II respectively, while gel filtration showed the molecular weight to be 114,000 for both types of the enzyme. The p/s for I and II were 7.9 and 8.1, respectively. The activities of both enzymes were inhibited by Ag+ and iodoacetic acid.

引用

页码：460 / 464

页数：5

共 25 条

[21] STUDIES ON LYTIC ENZYME ON FUNGAL CELL-WALL .5. PURIFICATIONS AND SOME PROPERTIES OF 2 CHITINASES FROM STREPTOMYCES-ORIENTALIS WHICH LYSE RHIZOPUS CELL-WALL [J].