Structure and characteristics of an endo-β-1,4-glucanase, isolated from Trametes hirsuta, with high degradation to crystalline cellulose

被引：9

作者：

Nozaki, Kouichi ^{[1
]}

Seki, Takahiro ^{[1
]}

Matsui, Keiko ^{[1
]}

Mizuno, Masahiro ^{[1
]}

Kanda, Takahisa ^{[1
]}

Amano, Yoshihiko ^{[1
]}

机构：

[1] Shinshu Univ, Fac Engn, Dept Chem & Mat Engn, Nagano 3808553, Japan

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 2007年 / 71卷 / 10期

关键词：

Trametes hirsuta; endoglucanase; cellulose degradation;

D O I：

10.1271/bbb.60385

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：

Trametes hirsuta produced cellulose-degrading enzymes when it was grown in a cellulosic medium such as Avicel or wheat bran. An endo-beta-1,4-glucanase (ThEG) was purified from the culture filtrate, and the gene and the cDNA were isolated. The gene consisted of an open reading frame encoding 384 amino acids, interrupted by 11 introns. The whole sequence showed high homology with that of family 5 glycoside hydrolase. The properties of the recombinant enzyme (rEG) in Aspergillus oryzae were compared with those of the En-1 from Irpex lacteus, which showed the highest homology among all the endoglucanases reported. The rEG activity against Avicel was about 8 times higher than that of En-1 when based on CMC degradation. A remarkable structural difference between the two enzymes was the length of the linker connecting the cellulose-binding domain to the catalytic domain.

引用

页码：2375 / 2382

页数：8

共 27 条

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