【摘 要】
：
β-Mannanase has been widely used in industries such as food and feed processing and thus has been a target enzyme for biotechnological development.In this
【机 构】
：
InstituteofMicrobialBiotechnology,JinanUniversity,GuangzhouCity,GuangdongProvince510632,ChinaInstitu
【出 处】
：
第九届国际分子模拟与信息技术应用学术会议(ICMS&I2018)
论文部分内容阅读
β-Mannanase has been widely used in industries such as food and feed processing and thus has been a target enzyme for biotechnological development.In this study,we sought to improve the stability and protease resistance of a recombinant β-mannanase,MAN47 from Armillariella tabescens,through rationally designed N-glycosylation.Based on homology modeling,molecular docking,secondary structure analysis and glycosylation feasibility analysis,an enhanced aromatic sequon sequence was introduced into specific MAN47 loop regions to facilitate N-glycosylation.The mutant enzymes were expressed in Pichia pastoris SMD1168,and their thermal stability,pH stability,trypsin resistance and pepsin resistance were determined.Two mutant MAN47 enzymes,g-123 and g-347,were glycosylated as expected when expressed in yeast,and their thermal stability,pH stability,and protease resistance were significantly improved compared to the wild-type enzyme.An enzyme with multiple stability characterizations has broad prospects in practical applications,and the rational design N-glycosylation strategy may have applications in simultaneously improving several properties of other biotechnological targets.
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