Amino acid substitutions in the N-terminus, cord and α-helix domains improved the thermostability of a family 11 xylanase XynR8.

Journal of Industrial Microbiology & Biotechnology
Huping XueHong Lu

Abstract

The thermostability of xylanase XynR8 from uncultured Neocallimastigales rumen fungal was improved by combining random point mutagenesis with site-directed mutagenesis guided by rational design, and a thermostable variant, XynR8_VNE, was identified. This variant contained three amino acid substitutions, I38V, D137N and G151E, and showed an increased melting temperature of 8.8 °C in comparison with the wild type. At 65 °C the wild-type enzyme lost all of its activity after treatment for 30 min, but XynR8_VNE retained about 65 % activity. To elucidate the mechanism of thermal stabilization, three-dimensional structures were predicted for XynR8 and its variant. We found that the tight packing density and new salt bridge caused by the substitutions may be responsible for the improved thermostability. These three substitutions are located in the N-terminus, cord and α-helix domains, respectively. Hence, the stability of these three domains may be crucial for the thermostability of family 11 xylanases.

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Citations

Oct 31, 2015·Applied Biochemistry and Biotechnology·Fucheng ZhuBingfang He
Apr 28, 2016·The Journal of General and Applied Microbiology·Chen-Yan ZhouJing Kang
Dec 29, 2020·International Journal of Biological Macromolecules·Apichet NgenyoungPongsak Khunrae
Aug 8, 2017·International Journal of Biological Macromolecules·Rafaela Zandonade VentorimValéria Monteze Guimarães
Apr 22, 2019·Current Opinion in Biotechnology·Casey A HookerKevin V Solomon
Aug 12, 2021·Brazilian Journal of Biology = Revista Brasleira De Biologia·B KalimR Ali

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