Characterization of a GH10 extremely thermophilic xylanase from the metagenome of hot spring for prebiotic production.

Autor: Yin YR; College of Agriculture and Biological Science, Dali University, Dali, 671003, People's Republic of China. yirui.yin@qq.com., Li XW; College of Agriculture and Biological Science, Dali University, Dali, 671003, People's Republic of China.; Key Laboratory of Bioinformatics and Computational Biology, Department of Education of Yunnan Province, Dali University, Dali, 671003, People's Republic of China., Long CH; College of Agriculture and Biological Science, Dali University, Dali, 671003, People's Republic of China., Li L; College of Agriculture and Biological Science, Dali University, Dali, 671003, People's Republic of China., Hang YY; College of Agriculture and Biological Science, Dali University, Dali, 671003, People's Republic of China., Rao MD; College of Agriculture and Biological Science, Dali University, Dali, 671003, People's Republic of China., Yan X; College of Agriculture and Biological Science, Dali University, Dali, 671003, People's Republic of China., Liu QL; College of Agriculture and Biological Science, Dali University, Dali, 671003, People's Republic of China., Sang P; College of Agriculture and Biological Science, Dali University, Dali, 671003, People's Republic of China.; Key Laboratory of Bioinformatics and Computational Biology, Department of Education of Yunnan Province, Dali University, Dali, 671003, People's Republic of China., Li WJ; College of Agriculture and Biological Science, Dali University, Dali, 671003, People's Republic of China. liwenjun3@mail.sysu.edu.cn.; State Key Laboratory of Biocontrol, Guangdong Provincial Key Laboratory of Plant Resources and Southern Marine Science and Engineering Guangdong Laboratory (Zhuhai), School of Life Sciences, Sun Yat-Sen University, Guangzhou, 510275, People's Republic of China. liwenjun3@mail.sysu.edu.cn., Yang LQ; College of Agriculture and Biological Science, Dali University, Dali, 671003, People's Republic of China. ylqbioinfo@163.com.; Key Laboratory of Bioinformatics and Computational Biology, Department of Education of Yunnan Province, Dali University, Dali, 671003, People's Republic of China. ylqbioinfo@163.com.
Jazyk: angličtina
Zdroj: Scientific reports [Sci Rep] 2023 Sep 25; Vol. 13 (1), pp. 16053. Date of Electronic Publication: 2023 Sep 25.
DOI: 10.1038/s41598-023-42920-6
Abstrakt: A xylanase gene (named xyngmqa) was identified from the metagenomic data of the Gumingquan hot spring (92.5 °C, pH 9.2) in Tengchong City, Yunnan Province, southwest China. It showed the highest amino acid sequence identity (82.70%) to endo-1,4-beta-xylanase from Thermotoga caldifontis. A constitutive expression plasmid (denominated pSHY211) and double-layer plate (DLP) method were constructed for cloning, expression, and identification of the XynGMQA gene. The XynGMQA gene was synthesized and successfully expressed in Escherichia coli DH5α. XynGMQA exhibited optimal activity at 90 °C and pH 4.6, being thermostable by maintaining 100% of its activity after 2 h incubated at 80 °C. Interestingly, its enzyme activity was enhanced by high temperatures (70 and 80 °C) and low pH (3.0-6.0). About 150% enzyme activity was detected after incubation at 70 °C for 20 to 60 min or 80 °C for 10 to 40 min, and more than 140% enzyme activity after incubation at pH 3.0 to 6.0 for 12 h. Hydrolytic products of beechwood xylan with XynGMQA were xylooligosaccharides, including xylobiose (X2), xylotriose (X3), and xylotetraose (X4). These properties suggest that XynGMQA as an extremely thermophilic xylanase, may be exploited for biofuel and prebiotic production from lignocellulosic biomass.
(© 2023. Springer Nature Limited.)
Databáze: MEDLINE
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