Purification and properties of chitinase from Arthrobacter sp NHB-10

被引:7
|
作者
Okazaki, K [1 ]
Kawabata, T
Nakano, M
Hayakawa, S
机构
[1] Kagawa Univ, Fac Agr, Dept Life Sci, Kagawa 7610795, Japan
[2] Kagawa Univ, Fac Agr, Dept Biochem & Food Sci, Kagawa 7610795, Japan
关键词
chitinase; Arthrobacter; chitin;
D O I
10.1271/bbb.63.1644
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
A chitinase was purified from the culture filtrate of nigeran-degrading Arthrobacter sp. NHB-10 by precipitation with ammonium sulfate and column chromatographies on DEAE-Sephadex A-50 and Superose 12. The final preparation was homogenous in polyacrylamide gel electrophoresis. The molecular weight of the purified enzyme was 30,000 and its isoelectric point was 6.8. The optimum pH and temperature for the enzyme activity were 5.0 and 45 degrees C, respectively. The enzyme was stable from pH 3 to 7 and up to 55 degrees C. The enzyme activity was inhibited by Hg2+ and p-chloromercuribenzoic acid. Two internal amino acid sequences of the enzyme were AGPQLLTGW and IGGVMT.
引用
收藏
页码:1644 / 1646
页数:3
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