Mutagenesis of N-terminal residues confer thermostability on a Penicillium janthinellum MA21601 xylanase

Mutagenesis of N-terminal residues confer thermostability on a Penicillium janthinellum MA21601 xylanase

Abstract Background A mesophilic xylanase PjxA from Penicillium janthinellum MA21601 has high specific activity under acidic condition and holds great potential for applications in the animal feed industry. To enhance the thermostability of xylanase PjxA, two mutation strategies in the N-terminal re...

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Bibliographic Details
Main Authors: Ke Xiong, Jie Hou, Yuefeng Jiang, Xiuting Li, Chao Teng, Qin Li, Guangsen Fan, Ran Yang, Chengnan Zhang
Format: Article
Language:English
Published: BMC 2019-07-01
Series:BMC Biotechnology
Subjects:
Endo-1
4-β-xylanase
Thermostability
N-terminal region
Disulfide bridge
Enzyme mutation
Online Access:http://link.springer.com/article/10.1186/s12896-019-0541-7

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http://link.springer.com/article/10.1186/s12896-019-0541-7

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