Abstract

Two highly active trifunctional hemicellulases were constructed by linking the catalytic portion of a xylanase with an arabinofuranosidase and a xylosidase, using either flexible peptide linkers or linkers containing a cellulose-binding domain. The multifunctional enzymes retain the parental enzyme properties and exhibit synergistic effects in hydrolysis of natural xylans and corn stover.

Document Type

Article

Publication Date

3-2009

Notes/Citation Information

Published in Applied and Environmental Microbiology, v. 75, no. 6, p. 1754-1757.

Copyright © 2009, American Society for Microbiology. All Rights Reserved.

The copyright holder has granted the permission for posting the article here.

Digital Object Identifier (DOI)

https://doi.org/10.1128/AEM.02181-08

Funding Information

This work was supported by a grant from the U.S. Department of Agriculture to L.Y. (2006-35504-17413).

Related Content

Supplemental material for this article may be found at http://aem.asm.org/.

ASM_75-6_1754-1757_Supplemental_Information.doc (33 kB)
Supplemental Information: Data on PCR primers used in construction of the multimeric enzymes (Table S1) and construction of the multimeric enzymes (AXX and CBD-AXX).

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