Shipin gongye ke-ji (Feb 2022)

Enzymatic Characterization of Xylanase TgXyn2

  • Yuhang GE,
  • Meixi CHEN,
  • Bo SUN,
  • Songna WU,
  • Qun WAN

DOI
https://doi.org/10.13386/j.issn1002-0306.2021060100
Journal volume & issue
Vol. 43, no. 4
pp. 138 – 144

Abstract

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Objectives: This study aimed to discover a acidic xylanase TgXyn2 with high enzymatic activities at low temperatures, which might have potential application in food industry. Method: TgXyn2 was heterologously expressed in E.coli with the expression vector pCold-TF. Results: The optimum reaction condition of TgXyn2 was 35 ℃ and pH5.0, respectively. Its Km was 1.287 μmol L−1 and Vmax was 2.083 μmol min−1 mg−1. Homology modeling showed that TgXyn2 had two antiparallel β-sheets and an α-helix, which was typical for the GH11 family. Conclusions: TgXyn2 had good enzymatic activities, which has potential application in food industry.

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