Enzymatic properties of acid resistant xylanase from Bacillus amyloliquefaciens
ZHENG Yalun1,4, XIA Ying1,4, LI Liang2, DONG Xiaoyuan3, FANG Shangling1,4, CHEN Maobin1,4, LI Qin1,4*
1(School of food and Biological engineering, Hubei University of Technology, Wuhan 430070, China) 2(Huanghelou Liquor Company Limited, Wuhan 430050, China) 3(Wuhan yashibo Technology Company Limited, Wuhan 430061, China) 4(Center for Brewing Technology & Equipment Research, Hubei University of Technology, Wuhan 430070, China)
Abstract: Xylanase is a type of hydrolytic enzyme that can catalyze the hydrolysis of xylan in plant hemicellulose, it is widely used in various industries and the market now has higher requirements for its production and activity. A xylanase gene was cloned from Bacillus amyloliquefaciens and heterogenous expressed in Escherichia coli. Isopropyl-β-D-thiogalactoside (IPTG) was adopted to induce the expression of recombinate strain BA-TB-1 and response surface experiments were designed to optimize the expression conditions. The predicted activity and experimental activity were 550.139 and 548.87 U/mL, respectively, indicating that it was feasible to apply response surface method to optimize the expression conditions of xylanase. Further results showed that xylanase had relatively high enzyme activity at pH 5.0 to 6.0, proving a good acid-resistant property. Incubated at 37℃, pH 5.0 and pH 5.0-7.0 for 1 h, the residual enzyme activity remained above 68% and 50%, respectively. The results lay some foundation for the mass production of acidic xylanase.
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