【摘 要】
：
Escherichia coli phytase appA belongs to the histidine acid phosphatase family.With a high hydrolytic activity towards phytate and resistant to pepsin digestion,it has been widely used as an animal fo
【机 构】
：
Key Laboratory of Chemical Biology and Molecular Engineering of Ministry of Education,Institute of B
【出 处】
：
中国生物化学与分子生物学会第十二届会员代表大会暨2018年全国学术会议
论文部分内容阅读
Escherichia coli phytase appA belongs to the histidine acid phosphatase family.With a high hydrolytic activity towards phytate and resistant to pepsin digestion,it has been widely used as an animal food additive.In order to study the effects of N-glycosylation,the recombinant appA-WT with 3 N-glycosylation sites,its N-glycosylation site deletion mutants(appAMut1,appA-Mut2,appA-Mut3)and over-glycosylated mutants(appA-Mut4 with 5 N-glycosylation sites,appA-Mut5 with 8 N-glycosylation sites)were constructed and expressed by Pichia pastoris for biochemical characterization.
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