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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Bibliografiset tiedot

Päätekijät:	Ke Xiong, Jie Hou, Yuefeng Jiang, Xiuting Li, Chao Teng, Qin Li, Guangsen Fan, Ran Yang, Chengnan Zhang
Aineistotyyppi:	Artigo
Kieli:	Inglês
Julkaistu:	BMC 2019-07-01
Sarja:	BMC Biotechnology
Aiheet:	Endo-1 4-β-xylanase Thermostability N-terminal region Disulfide bridge Enzyme mutation
Linkit:	http://link.springer.com/article/10.1186/s12896-019-0541-7
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