Identification of a Key Loop for Tuning Transglycosylation Activity in the Substrate-Binding Region of a Chitosanase
文献类型： 外文期刊
作者： Sun, Huihui 1 ; Zhao, Ling 1 ; Mao, Xiangzhao 2 ; Cao, Rong 1 ; Liu, Qi 1 ;
作者机构： 1.Chinese Acad Fishery Sci, Yellow Sea Fisheries Res Inst, Dept Food Engn & Nutr, Qingdao 266071, Peoples R China
2.Ocean Univ China, Coll Food Sci & Engn, Qingdao 266003, Peoples R China
3.Qingdao Natl Lab Marine Sci & Technol, Lab Marine Drugs & Bioprod, Qingdao 266237, Peoples R China
关键词： chitosanase; substrate binding; X-ray structure; GH46 family; transglycosylation activity
期刊名称：JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY （ 影响因子：6.1； 五年影响因子：6.3 ）
ISSN： 0021-8561
年卷期： 2023 年 71 卷 14 期
页码：
收录情况： SCI
摘要： Csn-PD, a glycoside family 46 chitosanase from Paenibacillus dendritiformis, exhibits endotype hydrolysis of chitosan and produces (GlcN)2 as the major product. Here, we report the crystal structure of Csn-PD at 1.68 angstrom resolution. The structure contains 14 alpha-helices and two beta-strands that fold into two globular domains with the substrate bound between them. To evaluate the function of a loop in the substrate-binding region (residues 112-116, NDKHP), a mutant Csn-PDL1, in which this loop was deleted, was generated. Hydrolysis of chitosan by the mutant yielded chitooligosaccharides (COSs) with higher degrees of polymerization (DP) than the wild-type enzyme. Excitingly, (GlcN)6 was produced from smaller COSs via transglycosylation activity of the mutant. Hence, the catalytic performance of a chitosanase was altered by modification of a loop in the substrate-binding regions. Our novel data on a chitosanase with transglycosylation activity offer a promising way to produce COSs with high DP.
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