Journal
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 164, Issue -, Pages 184-192Publisher
ELSEVIER
DOI: 10.1016/j.ijbiomac.2020.07.079
Keywords
Xylosidase; Halo-tolerance; Organic solvent tolerance; Monosaccharide tolerance; Synergic effect
Funding
- National Key Research andDevelopment Program of China [2016YFE0113300]
- Key Laboratory of Industrial Fermentation Microbiology of Ministry of Education and Tianjin Key Lab of IndustrialMicrobiology (Tianjin University of Science and Technology) [2017KF002]
- innovative Research Teamof Tianjin Municipal Education Commission [TD13-5015]
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Xylosidases with tolerance to high concentration of salts, organic solvents, and enzyme hydrolytic products are preferential for industrial application but were rarely reported. In this study, a novel xylosidase XYL21 belong to glycoside hydrolase 39 was characterized with optimal temperature of 45 degrees C and optimal pH of 5.50. Different to other GH39 xylosidases, XYL21 had excellent tolerance to salts, the activity of which is not inhibited but slightly increased in 0.50-1.50 M NaCl. It is also tolerant to organic solvents, especially retaining 105.18% relative activity even in the presence of 15.00% (v/v) ethanol. Moreover, XYL21 was insensitive to the final lignocellulose hydrolysis products including glucose, xylose, arabinose, mannose and galactose, which retains 111.36% and 53.49% relative activity in 0.30 and 0.90 M xylose, respectively. Further structural modeling analysis indicated that its excellent tolerance may be attributed to its high structural flexibility caused by the high proportion of random coils. Furthermore, XYL21 had a wide substrate specificity to catalyze xylan and xylo-oligosaccharides, and it significantly cooperated with xylanase to improve the hydrolysis efficiency with 1.52-fold. Considering these unique properties, XYL21 is a good candidate for both basic research and various potential industrial applications such as seafood processing and bioethanol production. (C) 2020 Published by Elsevier B.V.
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