Characterization of a metagenome-derived thermostable xylanase from Tengchong hot spring

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...

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Bibliographic Details
Published in:Biomass conversion and biorefinery 2024-05, Vol.14 (9), p.10027-10034
Main Authors: Yin, Yi-Rui, Li, Lei, Yang, Run-Feng, Li, Xin-Wei, Liu, Hong-Yan, Sang, Peng, Yang, Li-Quan
Format: Article
Language:English
Subjects:
Amino acids
Biotechnology
E coli
Energy
Enzyme activity
Hot springs
Original Article
Renewable and Green Energy
Xylanase
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Summary: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.
ISSN:2190-6815
2190-6823
DOI:10.1007/s13399-022-03296-1