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• W2262820281 endingPage "66" @default.
• W2262820281 startingPage "59" @default.
• W2262820281 abstract "This study aimed to obtain xylanase exhibiting improved enzyme properties to satisfy the requirements for industrial applications. The baxA gene encoding Bacillus amyloliquefaciens xylanase A was mutated by error-prone touchdown PCR. The mutant, pCbaxA50, was screened from the mutant library by using the 96-well plate high-throughput screening method. Sequence alignment revealed the identical mutation point S138T in xylanase (reBaxA50) produced by the pCbaxA50. The specific activity of the purified reBaxA50 was 9.38 U/mg, which was 3.5 times higher than that of its parent expressed in Escherichia coli BL21 (DE3), named reBaxA. The optimum temperature of reBaxA and reBaxA50 were 55 °C and 50 °C, respectively. The optimum pH of reBaxA and reBaxA50 were pH 6 and pH 5, respectively. Moreover, reBaxA50 was more stable than reBaxA under thermal and extreme pH treatment. The half-life at 60 °C and apparent melting temperature of reBaxA50 were 9.74 min and 89.15 °C, respectively. High-performance liquid chromatography showed that reBaxA50 released xylooligosaccharides from oat spelt, birchwood, and beechwood xylans, with xylotriose as the major product; beechwood xylan was also the most thoroughly hydrolyzed. This study demonstrated that the S138T mutation possibly improved the catalytic activity and thermostability of reBaxA50." @default.
• W2262820281 created "2016-06-24" @default.
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• W2262820281 date "2016-05-01" @default.
• W2262820281 modified "2023-10-17" @default.
• W2262820281 title "Obtaining a mutant of Bacillus amyloliquefaciens xylanase A with improved catalytic activity by directed evolution" @default.
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• W2262820281 doi "https://doi.org/10.1016/j.enzmictec.2016.02.001" @default.
• W2262820281 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26992794" @default.
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