Abstract
A novel xylanase gene (denominated xynDRTY1) was identified from Tengchong hot spring by a metagenomic approach. Its amino acid sequence was 73.43% identical to a hypothetical protein from Bryobacterales bacterium. The codon-optimized XynDRTY1 gene was synthesized and overexpressed in Escherichia coli. The XynDRTY1 was purified by using Ni–NTA affinity chromatography. It exhibited activity with natural glycosides, such as beechwood xylan (21.2 ± 3 U/mg) and oat spelt xylan (8.2 ± 0.3 U/mg). Its optimum pH was determined to be 6.0 and optimum temperature of 65 ℃, along with its stability over 140% and 110% relative enzyme activity after incubation at 60 ℃ for 20 min and 120 min, respectively. Based on these findings, we believe that XynDRTY1, as thermostable xylanase, may prove useful for biotechnological applications.
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Acknowledgements
We gratefully acknowledge Prof. Wen-Jun Li and his team from Sun Yat-sen University for their guidance on our metagenomic data compilation and analysis.
Funding
This research was supported by the National Natural Sciences Foundation of China Regional Program (Grant Nos. 31660015 and 31860243) and Yunnan Applied Basic Research Projects (Grant Nos. 202101AU070138, 2017FB024, and 2017FH001-032).
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YRY, PS, and LQY conceived the study. YRY and WH cloned the gene and cultured strains. RFY and HYL purified the recombinant protein. LL measured enzymatic activity. XWL and ZLL performed the data analysis and mapping. YRY, WH, PS, and LQY wrote the manuscript. All authors discussed the results and commented on the manuscript. All authors read and approved the final manuscript.
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Yin, YR., Li, L., Yang, RF. et al. Characterization of a metagenome-derived thermostable xylanase from Tengchong hot spring. Biomass Conv. Bioref. 14, 10027–10034 (2024). https://doi.org/10.1007/s13399-022-03296-1
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DOI: https://doi.org/10.1007/s13399-022-03296-1