Affiliation:
1. Guangxi Research Center for Microbial and Enzymatic Technology, College of Life Science and Technology, Guangxi University, Daxue Road No. 100, Nanning 530005, China
2. Guangxi Key Laboratory of Bio-Refinery, National Engineering Research Center for Non-Food Biorefinery, State Key Laboratory of Non-Food Biomass and Enzyme Technology, Guangxi Academy of Sciences, Daling Road No. 98, Nanning 530007, China
Abstract
Although β-xylosidases with xylanase activity are preferential for the hydrolysis of xylan and production of xylitol, reports on their use are scarce. In this study, a multifunctional β-xylosidase (XYL4) was identified. In addition to β-xylosidase activity, XYL4 also exhibited xylanase and low α-arabinosidase activity. The enzyme was able to hydrolyze bagasse xylan, oat spelt xylan, birchwood xylan, beechwood xylan, and corncob xylan, and showed the highest hydrolysis activity for corncob xylan. Structural modeling analysis indicated that XYL4 had an additional PA14 domain, which may play a key role in binding xylan substrates. Moreover, XYL4 was used to hydrolyze corncob xylan to produce xylose. When enzymatic hydrolysis and whole-cell catalysis were used to hydrolyze 100 g/L of corncob xylan, the xylose yields were 60.26% and 35.85%, respectively. Then, the Candida tropicalis was inoculated with the above hydrolysates for fermentation to produce xylitol. Using enzymatic hydrolysis and whole-cell catalysis, xylitol yields of 77.56% and 73.67% were obtained by C. tropicalis after the optimization of fermentation, respectively.
Funder
Guangxi Innovation-driven Development Major Science and Technology Innovation Base Construction Project
Guangxi Chair Technology Fund
National Natural Science Foundation of China
Subject
Plant Science,Biochemistry, Genetics and Molecular Biology (miscellaneous),Food Science
Cited by
1 articles.
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