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.
Publication types
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Amino Acid Sequence
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Biomass*
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Endo-1,4-beta Xylanases / genetics
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Endo-1,4-beta Xylanases / metabolism
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Glycoside Hydrolases / genetics
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Glycoside Hydrolases / metabolism*
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Molecular Sequence Data
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Xylans / metabolism*
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Xylosidases / genetics
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Xylosidases / metabolism
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Zea mays / metabolism*
Substances
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Recombinant Fusion Proteins
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Xylans
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Glycoside Hydrolases
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Xylosidases
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hemicellulase
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alpha-N-arabinofuranosidase
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Endo-1,4-beta Xylanases