Complete saccharification of cellulose at high temperature using endocellulase and beta-glucosidase from Pyrococcus sp.
We investigated a potential for glucose production from cellulose material using two kinds of hyperthermophilic enzymes, endo-cellulase (EG) and beta-glucosidase (BGL). Two BGLs from hyperthermophile Pyrococcus furiosus and mesophile Aspergillus aculeatus were compared for complete hydrolysis of cellulose with P. horikoshii endo-cellulase (EGPh). The combination reactions by each BGL enzyme and EGPh could produce only glucose without the other oligosaccharides from phosphoric acid swollen Avicel (PSA). The combination of the both hyperthermophilic cellulases, BGLPf and EGPh, will be adaptable to high efficient system to produce glucose at high temperature.
National Institute of Advanced Industrial Science and Technology (AIST), Ikeda, Osaka, Japan.
Han-Woo
HW
Kim
Kazuhiko
K
Ishikawa
D019843:Archaeal Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001230:Aspergillus / Q000201:enzymology* / Q000235:genetics; D044602:Cellulases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D002482:Cellulose / Q000737:chemistry* / Q000378:metabolism; D005656:Fungal Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D005947:Glucose / Q000737:chemistry / Q000378:metabolism; D006358:Hot Temperature; D006868:Hydrolysis; D007700:Kinetics; D019711:Pyrococcus / Q000201:enzymology* / Q000235:genetics; D001617:beta-Glucosidase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D019843:Archaeal Proteins; D005656:Fungal Proteins; D002482:Cellulose; D044602:Cellulases; D001617:beta-Glucosidase; D005947:Glucose