Improvement in the Catalytic Properties of A GH 11 Xylanase AEx11A，from Aspergillus oryzae by Saturated Mutagenesis

doi:10.3969/j.issn.1673-1689.2020.05.005

Home > Archive>Volume 39, Issue 5, 2020 >31-37. DOI:10.3969/j.issn.1673-1689.2020.05.005

Improvement in the Catalytic Properties of A GH 11 Xylanase AEx11A，from Aspergillus oryzae by Saturated Mutagenesis
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                        10.3969/j.issn.1673-1689.2020.05.005
                    
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In order to improve the catalytic properties of AEx11A，a glycoside hydrolase（GH） family 11 xylanase from Aspergillus oryzae，the Thr⁹⁸，Asn¹⁰⁰，Val¹²⁴，Pro¹²⁹ and Ile¹³²-encoding codons in AEx11A were selected for saturated mutagenesis by whole-plasmid PCR technique. Then，the mutagenesis libraries of AEx11A were constructed by transforming these variants into E. coli BL21（DE3），respectively. Using the enzyme activity of xylanase as criterion，transformants having an increase of more than 30% in activities were selected from the libraries by DNS method. Two mutation sites（Thr⁹⁸ and Val¹²⁴） with remarkably increased enzyme activities were subjected to iterative saturation mutation（ISM） and the optimal mutant，AEx11^AT98D-V124Q，was selected. The specific activity and catalytic efficiency of purified AEx11^AT98D-V124Q were 3.04- and 2.74-fold those of AEx11A. An improvement in the thermostability of AEx11^AV124T was observed compared with that of AEx11A，while the temperature properties of the other two mutants almost had no changes.

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LIU Yan, ZHANG Ting, KAN Tingting, LI Jianfang, WU Minchen. Improvement in the Catalytic Properties of A GH 11 Xylanase AEx11A，from Aspergillus oryzae by Saturated Mutagenesis[J]. Journal of Food Science and Biotechnology,2020,39(5):31-37.

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