Abstract
Dilute-acid pretreatment liquor (PL) produced at NREL through a continuous screw-driven reactor was analyzed for sugars and other potential inhibitory components. Their inhibitory effects on enzymatic hydrolysis of Solka Floc were investigated. When the PL was mixed into the enzymatic hydrolysis reactor at 1:1 volume ratio, the glucan and xylan digestibility decreased by 63% and 90%, respectively. The tolerance level of the enzyme for each inhibitor was determined. Of the identified degradation components, acetic acid was found to be the strongest inhibitor for cellulase activity, as it decreased the glucan yield by 10% at 1 g/L. Among the sugars, cellobiose and glucose were found to be strong inhibitors to glucan hydrolysis, whereas xylose is a strong inhibitor to xylan hydrolysis. Xylo-oligomers inhibit xylan digestibility more strongly than the glucan digestibility. Inhibition by the PL was higher than that of the simulated mixture of the identifiable components. This indicates that some of the unidentified degradation components, originated mostly from lignin, are potent inhibitors to the cellulase enzyme. When the PL was added to a simultaneous saccharification and co-fermentation using Escherichia coli KO11, the bioprocess was severely inhibited showing no ethanol formation or cell growth.
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Acknowledgment
The authors gratefully acknowledge the financial support provided by NREL (subcontract: LCO-9-99343-01), and Alabama Center for Paper and Renewable Resources Engineering. We also wish to thank Richard Elander and Nick Nagle of NREL for providing the pretreated corn stover, Genencor-Danisco (Paulo Alto, CA) for the enzymes used in this study; and our colleagues Suchithra Gopakumar and Li Kang for their help with GC/MS analysis and lignin extraction experiments.
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Kothari, U.D., Lee, Y.Y. Inhibition Effects of Dilute-Acid Prehydrolysate of Corn Stover on Enzymatic Hydrolysis of Solka Floc. Appl Biochem Biotechnol 165, 1391–1405 (2011). https://doi.org/10.1007/s12010-011-9355-3
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DOI: https://doi.org/10.1007/s12010-011-9355-3