Functional analysis of a novel lytic polysaccharide monooxygenase from Streptomyces griseus on cellulose and chitin

被引：9
|
作者：
Sato, Kazuki [1 ]
Chiba, Daisuke [1 ]
Yoshida, Sayaka [1 ]
Takahashi, Mayu [1 ]
Totani, Kazuhide [1 ]
Shida, Yosuke [2 ]
Ogasawara, Wataru [2 ]
Nakagawa, Yuko S. [1 ]
机构：
[1] Ichinoseki Coll, Natl Inst Technol, Div Chem Engn & Biotechnol, Ichinoseki 0214151, Japan
[2] Nagaoka Univ Technol, Dept Bioengn, 1603-1 Kamitomioka, Nagaoka, Niigata 9402188, Japan
来源：
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | 2020年 / 164卷
关键词：
Lytic polysaccharide monooxygenases (LPMO); Streptomyces griseus; Cellulose; CARBOHYDRATE-BINDING MODULES; PLANT-CELL WALLS; CHITOOLIGOSACCHARIDES; CLEAVAGE;
D O I：
10.1016/j.ijbiomac.2020.08.015
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：
Lytic polysaccharide monooxygenases (LPMOs) are enzymes that degrade polysaccharides with an oxidative mechanism and contributed to the efficiency in biomass degradation by glycoside hydrolases (GHs). In this study, the substrate and reaction specificity of SgLPMO10A that was an auxiliary activity family 10 (AA10) enzyme with a carbohydrate binding module family 2 (CBM2) domain from Streptomyces griseus, was analyzed. This enzyme produced oxidized cello-oligosaccharides from cellulose and boosted cellulose degradation by cellulases. Detailed study of the AA10 and CBM2 domains revealed that the binding ability of SgLPMO10A depended on CBM2 and that only the AA10 domain functions more effectively in the presence of a certain amount of substrates. (C) 2020 Elsevier B.V. All rights reserved.
引用
收藏
页码：2085 / 2091
页数：7
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