Enzymatic Characterization of Xylanase TgXyn2

GE Yuhang; CHEN Meixi; SUN Bo; WU Songna; WAN Qun

doi:10.13386/j.issn1002-0306.2021060100

Volume 43 Issue 4

Feb. 2022

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Science and Technology of Food Industry > 2022 > 43(4): 138-144. > DOI: 10.13386/j.issn1002-0306.2021060100

GE Yuhang, CHEN Meixi, SUN Bo, et al. Enzymatic Characterization of Xylanase TgXyn2[J]. Science and Technology of Food Industry, 2022, 43(4): 138−144. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2021060100.

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Enzymatic Characterization of Xylanase TgXyn2

1.
School of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China
2.
College of Science, Nanjing Agricultural University, Nanjing 210095, China

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Received Date: June 16, 2021
Available Online: December 19, 2021

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Abstract

Abstract

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 K_m was 1.287 μmol L⁻¹ and V_max 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.
- Trichoderma guizhouense,
- xylanase,
- enzymatic activity,
- GH11,
- food industry

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References (32)

References

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