PURIFICATION, PROPERTIES, AND PARTIAL AMINO-ACID-SEQUENCE OF CHITINASE FROM A MARINE ALTEROMONAS SP STRAIN-O-7

被引：51

作者：

TSUJIBO, H ^{[1
]}

YOSHIDA, Y ^{[1
]}

MIYAMOTO, K ^{[1
]}

IMADA, C ^{[1
]}

OKAMI, Y ^{[1
]}

INAMORI, Y ^{[1
]}

机构：

[1] INST MICROBIAL CHEM,SHINAGAWA KU,TOKYO 141,JAPAN

来源：

CANADIAN JOURNAL OF MICROBIOLOGY | 1992年 / 38卷 / 09期

关键词：

MARINE BACTERIUM; ALTEROMONAS SP; CHITINASE;

D O I：

10.1139/m92-145

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：

Chitinase (EC 3.2.1.14) was isolated from the culture supernatant of a marine bacterium, Alteromonas sp. strain 0-7. The enzyme (Chi-A) was purified by anion-exchange chromatography (DEAE-Toyopearl 650 M) and gel filtration (Sephadex G-100). The purified enzyme showed a single band on sodium dodecyl sulfate polyacrylamide gel electrophoresis. The molecular size and pI of Chi-A were 70 kDa and 3.9, respectively. The optimum pH and temperature of Chi-A were 8.0 and 50-degrees-C, respectively. Chi-A was stable in the range of pH 5-10 up to 40-degrees-C. Among the main cations, such as Na+, K+, Mg2+, and Ca2+, contained in seawater, Mg2+ stimulated Chi-A activity. N-Bromosuccinimide and 2-hydroxy-5-nitrobenzyl bromide inhibited Chi-A activity. The amino-terminal 27 amino acid residues of Chi-A were sequenced. This enzyme showed sequence homology with chitinases from terrestrial bacteria such as Serratia marcescens QMB1466 and Bacillus circulans WL-12.

引用

页码：891 / 897

页数：7

共 20 条

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