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

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 f...

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Published inInternational journal of biological macromolecules Vol. 164; pp. 2085 - 2091
Main Authors Sato, Kazuki, Chiba, Daisuke, Yoshida, Sayaka, Takahashi, Mayu, Totani, Kazuhide, Shida, Yosuke, Ogasawara, Wataru, Nakagawa, Yuko S.
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.12.2020
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Summary: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. •SgLPMO10A that bind two polysaccharide biomass, cellulose and chitin•SgLPMO10A produced oxidized cello-oligosaccharides from cellulose.•SgLPMO10A boosted cellulose degradation by cellulases.•Two domains of SgLPMO10A were studied in details.•AA10 domain is best used in application for efficient enzymatic solubilization.
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ISSN:0141-8130
1879-0003
DOI:10.1016/j.ijbiomac.2020.08.015