Engineering of a multifunctional hemicellulase

Zhanmin Fan; Joshua R. Werkman; Ling Yuan

doi:10.1007/s10529-009-9926-3

Engineering of a multifunctional hemicellulase

Zhanmin Fan, Joshua R. Werkman, Ling Yuan

Research output: Contribution to journal › Article › peer-review

37 Scopus citations

Abstract

To engineer a multifunctional xylan-degrading enzyme, a chimera was created by fusing the xylanase domain of the Clostridium thermocellum xylanase (xynZ) and a dual functional arabinofuranosidase/xylosidase (DeAFc; from a compost starter mixture) through a flexible peptide linker. The xylanase domain of xynZ possesses previously unreported endoglucanase activity. The chimera, possessing the activities of xylanase, endoglucanase, arabinofuranosidase and xylosidase, was expressed in E. coli and purified. The chimera closely resembled the parental enzymes in pH, temperature optima and kinetics, and was more active than the parental enzyme mixture in the hydrolysis of natural xylans and corn stover.

Original language	English
Pages (from-to)	751-757
Number of pages	7
Journal	Biotechnology Letters
Volume	31
Issue number	5
DOIs	https://doi.org/10.1007/s10529-009-9926-3
State	Published - May 2009

Bibliographical note

Funding Information:
Acknowledgements We thank Drs. K. Wagschal and C. Lee of the U.S. Department of Agriculture for providing the DeAFc gene, technical support and helpful discussions. We also thank Dr. I. Maiti of the University of Kentucky for providing the Xyln gene and Dr. M. Montross for supplying the corn stover substrates. This work is supported by a grant from the U.S. Department of Agriculture to L.Y. (2006-35504-17413).

Funding

Acknowledgements We thank Drs. K. Wagschal and C. Lee of the U.S. Department of Agriculture for providing the DeAFc gene, technical support and helpful discussions. We also thank Dr. I. Maiti of the University of Kentucky for providing the Xyln gene and Dr. M. Montross for supplying the corn stover substrates. This work is supported by a grant from the U.S. Department of Agriculture to L.Y. (2006-35504-17413).

Funders	Funder number
U.S. Department of Agriculture	2006-35504-17413

Keywords

Arabinoxylans
Biomass conversion
Enzyme engineering
Hemicellulases
Multifunctional enzymes

ASJC Scopus subject areas

Biotechnology
Bioengineering
Applied Microbiology and Biotechnology

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10.1007/s10529-009-9926-3

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title = "Engineering of a multifunctional hemicellulase",

abstract = "To engineer a multifunctional xylan-degrading enzyme, a chimera was created by fusing the xylanase domain of the Clostridium thermocellum xylanase (xynZ) and a dual functional arabinofuranosidase/xylosidase (DeAFc; from a compost starter mixture) through a flexible peptide linker. The xylanase domain of xynZ possesses previously unreported endoglucanase activity. The chimera, possessing the activities of xylanase, endoglucanase, arabinofuranosidase and xylosidase, was expressed in E. coli and purified. The chimera closely resembled the parental enzymes in pH, temperature optima and kinetics, and was more active than the parental enzyme mixture in the hydrolysis of natural xylans and corn stover.",

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author = "Zhanmin Fan and Werkman, {Joshua R.} and Ling Yuan",

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N2 - To engineer a multifunctional xylan-degrading enzyme, a chimera was created by fusing the xylanase domain of the Clostridium thermocellum xylanase (xynZ) and a dual functional arabinofuranosidase/xylosidase (DeAFc; from a compost starter mixture) through a flexible peptide linker. The xylanase domain of xynZ possesses previously unreported endoglucanase activity. The chimera, possessing the activities of xylanase, endoglucanase, arabinofuranosidase and xylosidase, was expressed in E. coli and purified. The chimera closely resembled the parental enzymes in pH, temperature optima and kinetics, and was more active than the parental enzyme mixture in the hydrolysis of natural xylans and corn stover.

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KW - Arabinoxylans

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KW - Enzyme engineering

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Engineering of a multifunctional hemicellulase

Abstract

Bibliographical note

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Keywords

ASJC Scopus subject areas

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