Properties and performance of glucoamylases for fuel ethanol production.
Studies were conducted on maltodextrin saccharification and on simultaneous saccharification and fermentation (SSF) with various commercial glucoamylases. In kinetics studies, none of the glucoamylases were able to completely convert maltodextrin into glucose. Typically, about 85% conversion was obtained, and glucose yields were about 75%. Typically, the kinetics were biphasic, with 1 h of rapid conversion, then a significant reduction in rate. Data were consistent with strong product inhibition and/or enzyme inactivation. Some glucoamylases followed first-order kinetics, initially slower at dextrin conversion, but eventually achieving comparable conversion and glucose concentrations. Most of the glucoamylases were more active at 55 degrees C than at 35 degrees C, but pH had little effect on activity. Screening studies in an SSF system demonstrated little difference between the glucoamylases, with a few exceptions. Subsequent targeted studies showed clear differences in performance, depending on the fermentation temperature and yeast used, suggesting that these are key parameters that would guide the selection of a glucoamylase.
Saville
Bradley A
BA
Department of Chemical Engineering and Applied Chemistry, University of Toronto, 200 College Street, Toronto, Ontario, Canada M5S 3E5. saville@chem-eng.utoronto.ca
Huang
Chunbei
C
Yacyshyn
Vince
V
Desbarats
Andrew
A
D019149:Bioreactors / Q000382:microbiology; D003470:Culture Media / Q000737:chemistry / Q000378:metabolism; D004736:Energy-Generating Resources; D004789:Enzyme Activation; D000431:Ethanol / Q000737:chemistry* / Q000378:metabolism*; D005087:Glucan 1,4-alpha-Glucosidase / Q000737:chemistry*; D007700:Kinetics; D011134:Polysaccharides / Q000737:chemistry* / Q000378:metabolism*; D013696:Temperature; D015003:Yeasts / Q000378:metabolism*
D003470:Culture Media; D011134:Polysaccharides; D000431:Ethanol; D005087:Glucan 1,4-alpha-Glucosidase