Asn57 N-glycosylation promotes the degradation of hemicellulose by beta-1,3-1,4-glucanase from Rhizopus homothallicus

文献类型： 外文期刊

第一作者： Zha, Zi-Qian

作者： Zha, Zi-Qian;You, Shuai;Hu, Yang-Hao;Zhang, Fang;Chen, Yi-Wen;Wang, Jun;You, Shuai;Wang, Jun

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关键词： beta-1,3-1,4-Glucanase; Hemicellulose; Rhizopus homothallicus; N-glycosylation; Thermostability; Catalytic activity

期刊名称：ENVIRONMENTAL SCIENCE AND POLLUTION RESEARCH （ 影响因子：5.19； 五年影响因子：5.053 ）

ISSN： 0944-1344

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收录情况： SCI

摘要： N-glycosylation alters the properties of different enzymes in different ways. Rhizopus homothallicus was first described as an environmental isolate from desert soil in Guatemala. A new gene encoding glucanase RhGlu146B was identified in R. homothallicus. It had high specific activity (9673 U/mg) when barley glucan was used as a substrate, and beta-glucan is hemicellulose that is abundant in nature. RhGlu16B has only one N-glycosylation site in its Ala55-Gly64 loop. It was found that N-glycosylation increased its T-m value and catalytic efficiency by 5.1 degrees C and 59%, respectively. Adding N-glycosylation to the same region of GH16 family glucanases TlGlu16A (from Talaromyces leycettanus) increased its thermostability and catalytic efficiency by 6.4 degrees C and 38%, respectively. In a verification experiment using GH16 family glucanases BisGlu16B (from Bisporus) in which N-glycosylation was removed, N-glycosylation also appeared to promote thermostability and catalytic efficiency. N-glycosylation reduced the overall root mean square deviation of the enzyme structure, creating rigidity and increasing overall thermostability. This study provided a reference for the molecular modification of GH16 family glucanases and guided the utilization of beta-glucan in hemicellulose.

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