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Enzymatic Characterization of Xylanase TgXyn2
- Source :
- Shipin gongye ke-ji, Vol 43, Iss 4, Pp 138-144 (2022)
- Publication Year :
- 2022
- Publisher :
- The editorial department of Science and Technology of Food Industry, 2022.
-
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 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.
Details
- Language :
- Chinese
- ISSN :
- 10020306
- Volume :
- 43
- Issue :
- 4
- Database :
- Directory of Open Access Journals
- Journal :
- Shipin gongye ke-ji
- Publication Type :
- Academic Journal
- Accession number :
- edsdoj.7b53c3c5d033447fb02eb17f7c351c6d
- Document Type :
- article
- Full Text :
- https://doi.org/10.13386/j.issn1002-0306.2021060100