Functional characterization of three GH10 xylanases

Park, Jesslyn; Glasgow, Evan; Fox, Brian G.

doi:10.1096/fasebj.31.1_supplement.607.1

Title: Functional characterization of three GH10 xylanases

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Abstract

Decreased availability of fossil fuels has driven an increased demand for sustainable energy sources such as biofuels. One area of bioenergy research involves development of biocatalysts able to efficiently degrade biomass “waste”‐products, such as substrates derived from corn stover, rather than easily‐fermentable biomass used for food, such as starch from corn kernels. Xylanases are of interest for their ability to hydrolyze hemicellulosic sugars found in plant cell walls, allowing utilization of waste‐derived biomass. In this study, three xylanases of glycoside hydrolase family 10 (GH10) are functionally characterized and optimized for temperature and pH, as well as kinetically analyzed for xylose monomer and oligomer production. These enzymes, GH10‐4, GH10‐9, and GH10‐15, demonstrate activity upon substrates xylan and arabinoxylan. For GH10‐4, optima are 50°C at pH 8 on xylan and 45°C at pH 8 on arabinoxylan. For GH10‐9, optima are 70°C at pH 5 on xylan and 70°C at pH 5 on arabinoxylan. For GH10‐15, optima are 50°C at pH 8 on xylan and 45°C at pH 5 on arabinoxylan. Kinetic analysis reveals GH10‐4 produces xylose (X1), xylobiose (X2), xylotriose (X3), xylotetraose (X4), and xylopentaose (X5) from xylan, while GH10‐9 and GH10‐15 produce X1, X2, and X3. From arabinoxylan, GH10‐4 produces X1,more »« less

Authors:

Park, Jesslyn ^[1]; Glasgow, Evan ^[2]; Fox, Brian G. ^[2]

Department of Chemistry, Physics, and Geology Winthrop University Rock Hill SC
Department of Biochemistry University of Wisconsin ‐ Madison Madison WI

Publication Date:: Wed Oct 03 00:00:00 EDT 2018

Sponsoring Org.:: USDOE

OSTI Identifier:: 1787054

Resource Type:: Publisher's Accepted Manuscript

Journal Name:: FASEB Journal

Additional Journal Information:: Journal Name: FASEB Journal Journal Volume: 31 Journal Issue: S1; Journal ID: ISSN 0892-6638

Publisher:: FASEB

Country of Publication:: United States

Language:: English

Citation Formats


                    Park, Jesslyn, Glasgow, Evan, and Fox, Brian G. Functional characterization of three GH10 xylanases.  United States: N. p., 2018. 
Web.  doi:10.1096/fasebj.31.1_supplement.607.1.

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                    Park, Jesslyn, Glasgow, Evan, & Fox, Brian G. Functional characterization of three GH10 xylanases.  United States.  https://doi.org/10.1096/fasebj.31.1_supplement.607.1

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                    Park, Jesslyn, Glasgow, Evan, and Fox, Brian G. Wed .  
"Functional characterization of three GH10 xylanases".  United States.  https://doi.org/10.1096/fasebj.31.1_supplement.607.1.

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@article{osti_1787054,

  title        = {Functional characterization of three GH10 xylanases},

  author       = {Park, Jesslyn and Glasgow, Evan and Fox, Brian G.},

  abstractNote = {Decreased availability of fossil fuels has driven an increased demand for sustainable energy sources such as biofuels. One area of bioenergy research involves development of biocatalysts able to efficiently degrade biomass “waste”‐products, such as substrates derived from corn stover, rather than easily‐fermentable biomass used for food, such as starch from corn kernels. Xylanases are of interest for their ability to hydrolyze hemicellulosic sugars found in plant cell walls, allowing utilization of waste‐derived biomass. In this study, three xylanases of glycoside hydrolase family 10 (GH10) are functionally characterized and optimized for temperature and pH, as well as kinetically analyzed for xylose monomer and oligomer production. These enzymes, GH10‐4, GH10‐9, and GH10‐15, demonstrate activity upon substrates xylan and arabinoxylan. For GH10‐4, optima are 50°C at pH 8 on xylan and 45°C at pH 8 on arabinoxylan. For GH10‐9, optima are 70°C at pH 5 on xylan and 70°C at pH 5 on arabinoxylan. For GH10‐15, optima are 50°C at pH 8 on xylan and 45°C at pH 5 on arabinoxylan. Kinetic analysis reveals GH10‐4 produces xylose (X1), xylobiose (X2), xylotriose (X3), xylotetraose (X4), and xylopentaose (X5) from xylan, while GH10‐9 and GH10‐15 produce X1, X2, and X3. From arabinoxylan, GH10‐4 produces X1, X2, X3, X4, while GH10‐9 and GH10‐15 produce X1, X2, X3. Conclusive kinetic data may suggest applicability of these enzymes for industrial use within biocatalysts and contribute further insight to the functionality of enzymes within GH10. Support or Funding Information The authors are grateful for financial support by the Integrated Biological Sciences Summer Research Program (IBS‐SRP, NSF) at the University of Wisconsin‐Madison and the Great Lakes Bioenergy Research Center (GLBRC) of the U.S. Department of Energy. Presentation travel support is provided by the Ronald E. McNair Scholars Program of Winthrop University. The authors also thank Lai Bergeman, Craig Bingman, Bob Smith, Emily Beebe, Kirk Vander Meulen, Amber Smith, David Wassarman, and John Greenler for professional support.},

  doi          = {10.1096/fasebj.31.1_supplement.607.1},

  journal      = {FASEB Journal},

  number       = S1,

  volume       = 31,

  place        = {United States},

  year         = {Wed Oct 03 00:00:00 EDT 2018},

  month        = {Wed Oct 03 00:00:00 EDT 2018}

}

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