新型灰色链霉菌裂解多糖单加氧酶在纤维素和几丁质上的功能分析。
Functional analysis of a novel lytic polysaccharide monooxygenase from Streptomyces griseus on cellulose and chitin.
机构信息
Division of Chemical Engineering and Biotechnology, National Institute of Technology, Ichinoseki College, Ichinoseki 021-8511, Japan.
Department of Bioengineering, Nagaoka University of Technology, 1603-1 Kamitomioka, Nagaoka, Niigata 940-2188, Japan.
出版信息
Int J Biol Macromol. 2020 Dec 1;164:2085-2091. doi: 10.1016/j.ijbiomac.2020.08.015. Epub 2020 Aug 4.
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.
溶细胞寡糖单加氧酶（LPMOs）是一种通过氧化机制降解多糖的酶，有助于糖苷水解酶（GHs）提高生物质的降解效率。在这项研究中，对来自灰色链霉菌的辅助活性家族 10（AA10）酶和碳水化合物结合模块家族 2（CBM2）结构域的 SgLPMO10A 的底物和反应特异性进行了分析。该酶从纤维素中产生氧化的纤维寡糖，并通过纤维素酶促进纤维素的降解。对 AA10 和 CBM2 结构域的详细研究表明，SgLPMO10A 的结合能力取决于 CBM2，并且只有在存在一定量的底物时，AA10 结构域才能更有效地发挥作用。
Zotero 插件