Purification and some properties of an endo-1,4-beta-D-mannanase from a marine mollusc, Littorina brevicula

被引：20

作者：

Yamaura, I

Nozaki, Y

Matsumoto, T

Kato, T

机构：

[1] Technology Development Laboratories, Takeda Chemical Industries Ltd, Osaka, 532, Yodogawa-ku

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 1996年 / 60卷 / 04期

关键词：

marine mollusc enzyme; Littorina brevicula; beta-1,4-mannanase; N-terminal sequence;

D O I：

10.1271/bbb.60.674

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：

An endo-1,4-beta-D-mannanase (EC 3.2.1.78) was purified from viscera of a marine mollusc, Littorina brevicula. The purified enzyme, with a molecular weight of 42,000, was homogeneous by SDS-PAGE. The amino-terminal sequence starting with Gly was analyzed up to the 30th amino acid. The enzyme was stable from pH about 4.0 to about 9.0 and had its maximum activity at pH about 6.5. The purified enzyme produced M2, M3, M4, and M5 from Codium beta-1,4-mannan. The enzyme activity was greatly inhibited by Ag+, Hg2+, Cu2+, and N-bromosuccinimide at 1 mM concentration.

引用

页码：674 / 676

页数：3

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