Improving the temperature characteristics and catalytic efficiency of a mesophilic xylanase from Aspergillus oryzae, AoXyn11A, by iterative mutagenesis based on in silico design.

ABSTRACT: To improve the temperature characteristics and catalytic efficiency of a glycoside hydrolase family (GHF) 11 xylanase from Aspergillus oryzae (AoXyn11A), its variants were predicted based on in silico design. Firstly, Gly²¹ with the maximum B-factor value, which was confirmed by molecular dynamics (MD) simulation on the three-dimensional structure of AoXyn11A, was subjected to site-saturation mutagenesis. Thus, one variant with the highest thermostability, AoXyn11A^G21I, was selected from the mutagenesis library, E. coli/Aoxyn11A ^G21X (X: any one of 20 amino acids). Secondly, based on the primary structure multiple alignment of AoXyn11A with seven thermophilic GHF11 xylanases, AoXyn11A^Y13F or AoXyn11A^G21I-Y13F, was designed by replacing

SUBMITTER: Li XQ 

PROVIDER: S-EPMC5432455 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature