PURIFICATION AND SOME PROPERTIES OF CHITINASE FROM THE STOMACH OF JAPANESE EEL, ANGUILLA-JAPONICA

被引:23
作者
KONO, M
MATSUI, T
SHIMIZU, C
KOGA, D
机构
[1] UNIV TOKYO, FAC AGR, MARINE BIOCHEM LAB, TOKYO 113, JAPAN
[2] YAMAGUCHI UNIV, FAC AGR, BIOCHEM LAB, YAMAGUCHI 753, JAPAN
来源
AGRICULTURAL AND BIOLOGICAL CHEMISTRY | 1990年 / 54卷 / 04期
关键词
D O I
10.1080/00021369.1990.10870054
中图分类号
S3 [农学(农艺学)];
学科分类号
0901 ;
摘要
Chitinase (EC 3.2.1.14) was purified from the stomach of Japanese eel, Anguilla japonica, by fractionations with ammonium sulfate, Sephadex G-100 gel filtration, and DEAE-cellulose, CM-cellulose, and hydroxylapatite column chromatography. The molecular weight of this enzyme was 50,000 by SDS-PAGE, and the optimum pH was 4.4. The activity was strongly inhibited by Hg2+ and slightly activated by EDTA. The hydrolysis products of colloidal chitin by the enzyme were GlcNAc and GlcNAc2. When GlcNAc3–6 was used as substrate, GlcNAc and GlcNAc2 were recognized as final products with various ratios. GlcNAc2 was not hydrolyzed by this chitinase. © 1990 by the Japan Society for Bioscience, Biotechnology, and Agrochemistry. All rights reserved.
引用
收藏
页码:973 / 978
页数:6
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