Multimeric hemicellulases facilitate biomass conversion.
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.
Fan
Zhanmin
Z
Department of Plant and Soil Sciences, and Kentucky Tobacco Research and Development Center, University of Kentucky, Cooper and University Drives, Lexington, KY 40546, USA.
Wagschal
Kurt
K
Chen
Wei
W
Montross
Michael D
MD
Lee
Charles C
CC
Yuan
Ling
L
D000595:Amino Acid Sequence; D018533:Biomass; D043364:Endo-1,4-beta Xylanases / Q000235:genetics / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D014990:Xylans / Q000378:metabolism*; D014995:Xylosidases / Q000235:genetics / Q000378:metabolism; D003313:Zea mays / Q000378:metabolism*
D011993:Recombinant Fusion Proteins; D014990:Xylans; D006026:Glycoside Hydrolases; D014995:Xylosidases; C023305:hemicellulase; C019713:alpha-N-arabinofuranosidase; D043364:Endo-1,4-beta Xylanases