Heterologous expression, characterization and application of a new β-xylosidase identified in solventogenic Clostridium sp. strain BOH3.

Saved in:
Bibliographic Details
Title: Heterologous expression, characterization and application of a new β-xylosidase identified in solventogenic Clostridium sp. strain BOH3.
Authors: Li, Tinggang1, Wu, Yi-Rui1, He, Jianzhong1 jianzhong.he@nus.edu.sg
Source: Process Biochemistry. Apr2018, Vol. 67, p99-104. 6p.
Subjects: Xylosidases, Clostridium, Gene expression, Glycosidases, Hydrolysis, Escherichia coli
Abstract: A β-xylosidase gene (Bxyl BOH3 ) was identified in a solventogenic bacterium Clostridium sp. strain BOH3, which is a member of the glycoside hydrolase family 43 (GH43). The recombinant enzyme of Bxyl BOH3 was expressed in Escherichia coli with a high specific activity of 48.7 U/mg and a low K m value of 2.71 mM at an optimal temperature of 40 °C and pH of 5.0-6.0, indicating its high affinity for the substrate and enzymatic potency. Moreover, activity of β-xylosidase can be enhanced (>1.6 times) by addition of Zn 2+ . The concentration of reducing sugar (including xylose and xylooligosaccharides) with the synergism of xylanase and recombinant β-xylosidase was enhanced up to 129.8% (11.93 g/L) after hydrolysis of 30 g/L of xylan for 24 h when comparing with only xylanase (9.19 g/L). Application of this recombinant β-xylosidase together with xylanase improved xylan hydrolysis efficiency, thus leading to increased biofuels productivity from xylan fermented by Clostridium species. [ABSTRACT FROM AUTHOR]
Copyright of Process Biochemistry is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Engineering Source
Be the first to leave a comment!
You must be logged in first