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Novel Aspergillus hemicellulases enhance performance of commercial cellulases in lignocellulose hydrolysis
Author(s) -
Shin HyunDong,
Vo Trinh,
Chen Rachel
Publication year - 2011
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1002/btpr.547
Subject(s) - xylanase , cellulase , chemistry , xylan , food science , hydrolysis , glycoside hydrolase , biochemistry , aspergillus fumigatus , reducing sugar , beta glucosidase , enzyme , microbiology and biotechnology , sugar , biology
A novel hemicellulase‐producing fungal strain was isolated from a local soil sample. The organism is identified as Aspergillus fumigatus based on ribosomal RNA analyses. The Aspergillus strain, designated as 2NB, produces both enzymes acting on xylan backbone (xylanase and β‐xylosidase), and those acting on side chains (or accessory enzymes) notably α‐arabinofuranosidase and acetyl‐xylan esterase. The Asperigillus hemicellulases are characterized as having relatively low xylanase and β‐xylosidase activities but high side chain removal activities. The activity ratio of side‐chain acting enzymes to xylanase is higher than that of the Multifect enzyme, a commercial hemicellulase product. The potential of the novel hemicellulases in lignocelluloses bioprocessing was demonstrated with alkaline‐pretreated switchgrass as lignocellulose substrate with hemicellulase supplemented with a ratio of xylanase activity to filter paper unit of 2:1. Supplement of Aspergillus hemicellulases to commercial cellulases significantly enhanced the hydrolysis of lignocellulose, achieving a 94% hydrolysis yield based on reducing sugar measurement, compared to 60% when no hemicellulase or 75% when Multifect enzyme was used under otherwise identical conditions. The significant improvement resulting from supplementing a hemicellulase mix with high side‐chain removal activities suggests the importance of accessory hemicellulases in lignocellulose processing. © 2011 American Institute of Chemical Engineers Biotechnol. Prog., 2011