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- Title
Loop结构引入半胱氨酸对木聚糖酶XynASP热稳定性的影响.
- Authors
陈康太; 杨思文; 刁梦月; 王宵宵; 郭双; 李恩中; 李同彪
- Abstract
In order to explore the effects of introducing cysteine into the Loop structure on the thermal stability of GH11 family xylanase, using the Loop structure of xylanase XynASP from Aspergillus saccharolyticus JOP 1030-1 as the research object, the mutant XynN95C was obtained by mutating asparagine (Asn) at site 95 to cysteine (Cys) by site-directed mutagenesis, and induced expression in Escherichia coli BL21(DE3). Enzymatic property analysis results showed that the optimum temperature of mutant XynN95C was 50 ℃, the half-life of the enzyme activity t1/240 ℃ was 38 min, which was 5 ℃ and 18 min higher than that of wild-type XynASP, and the optimum pH decreased from 6.0 to 5.0. In addition, the metal ion tolerance of XynN95C was stronger, the relative enzyme activity was 93.9% after treatment with Fe3+ for 1 h, which was significantly higher than that of wild type (65.9%). In conclusion, the introduction of cysteine into Loop structure could effectively improve the thermal stability of xylanases, which provided a new idea for the thermal stability modification of GH11 family xylanases.
- Subjects
SITE-specific mutagenesis; ENZYMATIC analysis; THERMAL stability; XYLANASES; FAMILY stability
- Publication
China Brewing, 2022, Vol 41, Issue 10, p106
- ISSN
0254-5071
- Publication type
Article
- DOI
10.11882/j.issn.0254-5071.2022.10.018