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Hydrolysis of filter‐paper cellulose to glucose by two recombinant endogenous glycosyl hydrolases of Coptotermes formosanus
Author(s) -
Zhang Dunhua,
Lax Alan R.,
Bland John M.,
Yu Jiujiang,
Fedorova Natalie,
Nierman William C.
Publication year - 2010
Publication title -
insect science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.991
H-Index - 45
eISSN - 1744-7917
pISSN - 1672-9609
DOI - 10.1111/j.1744-7917.2010.01321.x
Subject(s) - coptotermes , glycosyl , biology , cellulose , biochemistry , cellulase , cellobiose , cellulosic ethanol , hydrolysis , polysaccharide , glycoside hydrolase , bioconversion , recombinant dna , gene , botany , fermentation
Genes encoding for glycosyl hydrolases (GH) in multiple families were recovered from an expression sequence tag library of Coptotermes formosanus , a xylophagous lower termite species. Functional analyses of these genes not only shed light on the mechanisms the insect employs to successfully use cellulosic materials as energy sources, which may serve as strategic targets for designing molecular‐based bio‐pesticides, but also enrich discoveries of new cellulolytic enzymes for conversion of biomass into biofuel. Our study demonstrated that cellulose could be converted to glucose by two recombinant endogenous glycosyl hydrolases (endo‐β‐1,4 glucanase in GH9 and β‐glucosidase in GH1). While the former cleaved cellulose to cellobiose and cellotriose, the resulting simple cellodextrins were digested to glucose. Both of the Escherichia coli ‐expressed recombinant proteins showed properties that could be incorporated in a glucose‐based ethanol production program.