Multimeric hemicellulases facilitate biomass conversion.
- Resource Type
- Academic Journal
- Authors
- Fan 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 K; Chen W; Montross MD; Lee CC; Yuan L
- Source
- Publisher: American Society for Microbiology Country of Publication: United States NLM ID: 7605801 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1098-5336 (Electronic) Linking ISSN: 00992240 NLM ISO Abbreviation: Appl Environ Microbiol Subsets: MEDLINE
- Subject
- Language
- English
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.