Fusion of Phytase YiAPPA with the Raw-starch Binding Domain and Characterization of the Fusion Enzyme

doi:10.13560/j.cnki.biotech.bull.1985.2017-0795

Abstract

Abstract: This work aims to obtain a fusion enzyme with improved enzymatic properties comprised of phytase YiAPPA and raw-starch binding domain SBD. The raw-starch binding domain（SBD）of thermoacidophilic α-amylase GTamy was introduced into the C-terminal end of Yersinia intermedia phytase（YiAPPA）to generate a fusion enzyme YiAPPA-SBD. The fusion of YiAPPA with SBD resulted in improvements both in terms of thermal activity and stability. Besides，YiAPPA-SBD could absorb raw corn starch. Specifically，YiAPPA-SBD exhibited higher relative activity than YiAPPA within 55-90℃.The half-life of YiAPPA-SBD increased from 15 min to 30 min when incubated at 80℃. The adsorption efficiency of YiAPPA-SBD was 80% when the raw corn starch concentration was over 8%. Moreover，YiAPPA-SBD showed minor changes in its specific activity（3 900 U/mg）at optimal pH（pH 4.5），indicating that YiAPPA-SBD has solid pH stability and resistance to protease when compared to YiAPPA.

Key words: phytase YiAPPA, raw-starch binding domain, fusion enzyme, thermostability, raw-starch adsorption efficiency

YUAN Lin, HUANG Zhao, ZENG Jing, GUO Jian-jun, ZHANG Ting, Lü Jun. Fusion of Phytase YiAPPA with the Raw-starch Binding Domain and Characterization of the Fusion Enzyme[J]. Biotechnology Bulletin, 2018, 34(3): 200-207.

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