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Title of Journal: Biotechnol Lett

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Abbravation: Biotechnology Letters

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Springer Netherlands

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DOI

10.1002/9781444314380.ch15

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1573-6776

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Engineering the thermostability of a xylanase from

Authors: Zhongfa Chen Huimin Zhang Junqing Wang Cunduo Tang Jing Wu Minchen Wu
Publish Date: 2013/08/02
Volume: 35, Issue: 12, Pages: 2073-2079
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Abstract

A mesophilic Aspergillus oryzae xylanase AoXyn11A belongs to glycoside hydrolase family 11 Hydrogen bonds and a disulfide bridge were introduced between the Nterminus extension and the βsheet A2 of AoXyn11A which were located in the corresponding region of a hyperthermostable xylanase The mutants were designated as AoXyn11AC5 and AoXyn11AC5–C32 respectively The thermostabilities of AoXyn11A and the mutants were assessed by the molecular dynamics simulations After being incubated at 55 °C for 30 min AoXyn11AC5–C32 retained 49  of its original activity AoXyn11AC5 retained 12  and AoXyn11A retained 3  The interactions between the Nterminus extension and the βsheet A2 were analyzed in depth there was enhancement of the interactions between the Nterminus extension and the βsheet A2 of AoXyn11A that improved its thermostabilityThis work was financially supported by the National Nature Science Foundation of China No 31101229 Key Laboratory of Carbohydrate Chemistry Biotechnology Ministry of Education Jiangnan University No KLCCBKF201208 Doctoral Research Funds of Jiangnan University No JUDCF11032 and Postgraduate Innovation Training Project of Jiangsu No CXZZ120758 The authors are grateful to Prof Xianzhang Wu School of Biotechnology Jiangnan University for providing technical assistance

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