Activation of enzymatic chitin degradation by a lytic polysaccharide monooxygenase

被引:26
|
作者
Hamre, Anne Grethe [1 ]
Eide, Kristine B. [1 ]
Wold, Hanne H. [1 ]
Sorlie, Morten [1 ]
机构
[1] Norwegian Univ Life Sci, Dept Chem Biotechnol & Food Sci, N-1432 As, Norway
关键词
LPMO; Glycoside hydrolases; Kinetics; Rate enhancement; AA10; CBP21; SERRATIA-MARCESCENS BJL200; BINDING PROTEIN CBP21; CELLULOSE; SUBSTRATE; PROCESSIVITY; PURIFICATION; CONVERSION; ENZYMES;
D O I
10.1016/j.carres.2015.02.010
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
For decades, the enzymatic conversion of recalcitrant polysaccharides such as cellulose and chitin was thought to solely rely on the synergistic action of hydrolytic enzymes, but recent work has shown that lytic polysaccharide monooxygenases (LPMOs) are important contributors to this process. Here, we have examined the initial rate enhancement an LPMO (CBP21) has on the hydrolytic enzymes (ChiA, ChiB, and ChiC) of the chitinolytic machinery of Serratia marcescens through determinations of apparent k(cat) (k(cat)(app)) values on a beta-chitin substrate. k(cat)(app) values were determined to be 1.7 +/- 0.1 s(-1) and 1.7 +/- 0.1 s(-1) for the exo-active ChiA and ChiB, respectively and 1.2 +/- 0.1 s(-1) for the endo-active ChiC. The addition of CBP21 boosted the k(cat)(app) values of ChiA and ChiB giving values of 11.1 +/- 1.5 s(-1) and 13.9 +/- 1.4 s(-1), while there was no effect on ChiC (0.9 +/- 0.1 s(-1)). (C) 2015 Elsevier Ltd. All rights reserved.
引用
收藏
页码:166 / 169
页数:4
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