Functional analysis of α-1,3-glucanase domain structure from Streptomyces thermodiastaticus HF3-3

The Journal of General and Applied Microbiology

article

Niphawan Panti¹  Vipavee Cherdvorapong¹  Takafumi Itoh²  Takao Hibi²  Wassana Suyotha³  Shigekazu Yano⁴  Mamoru Wakayama¹ 

[1] Department of Biotechnology, Faculty of Life Sciences, Ritsumeikan University;Department of Bioscience and Biotechnology, Faculty of Bioscience and Biotechnology, Fukui Prefectural University;Biotechnology for Bioresource Utilization Laboratory, Department of Industrial Biotechnology, Faculty of Agro-industry, Prince of Songkla University;Department of Biochemical Engineering, Graduate School of Sciences and Engineering, Yamagata University

关键词: α-1;    3-glucanase;    α-1;    3-glucan-binding activity;    domain function;    mycodextranase;    Streptomyces thermodiastaticus;   

DOI  :  10.2323/jgam.2020.07.003

学科分类：微生物学和免疫学

来源: Applied Microbiology, Molecular and Cellulrar Biosciences Research Foundation

【 摘 要 】

α-1,3-Glucanase from Streptomyces thermodiastaticus HF3-3 (Agl-ST) has been classified in the glycoside hydrolase (GH) family 87. Agl-ST is a multi-modular domain consisting of an N -terminal β-sandwich domain (β-SW), a catalytic domain, an uncharacterized domain (UC), and a C -terminal discoidin domain (DS). Although Agl-ST did not hydrolyze α-1,4-glycosidic bonds, its amino acid sequence is more similar to GH87 mycodextranase than to α-1,3-glucanase. It might be categorized into a new subfamily of GH87. In this study, we investigated the function of the domains. Several fusion proteins of domains with green fluorescence protein (GFP) were constructed to clarify the function of each domain. The results showed that β-SW and DS domains played a role in binding α-1,3-glucan and enhancing the hydrolysis of α-1,3-glucan. The binding domains, β-SW and DS, also showed binding activity toward xylan, although it was lower than that for α-1,3-glucan. The combination of β-SW and DS domains demonstrated high binding and hydrolysis activities of Agl-ST toward α-1,3-glucan, whereas the catalytic domain showed only a catalytic function. The binding domains also achieved effective binding and hydrolysis of α-1,3-glucan in the cell wall complex of Schizophyllum commune .

【 授权许可】

Unknown