Replacing a suite of commercial pectinases with a single enzyme, pectate lyase B, in Saccharomyces cerevisiae fermentations of cull peaches
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Fermentation of pectin-rich biomass with low concentrations of polysaccharides requires some treatment of the pectin, but does not need complete degradation of the polysaccharide to reach maximum ethanol yields. Cull peaches, whole rotten fruits that are not suitable for sale, contain high concentrations of glucose (27.7 % dw) and fructose (29.3 % dw) and low amounts of cellulose (2.8 % dw), hemicellulose (4.5 % dw) and pectin (5.6 % dw). Amounts of commercial saccharification enzymes, cellulase and cellobiase can be significantly decreased and commercial pectinase mixtures can be replaced completely with a single enzyme, pectate lyase (PelB), while maintaining ethanol yields above 90 % of the theoretical maximum. PelB does not completely degrade pectin; it only releases short chain oligogalacturonides. However, the activity of PelB is sufficient for the fermentation process, and its addition to fermentations without commercial pectinase increases ethanol production by ~12 %.
KeywordsSaccharomyces cerevisiae PelB Glycome profile Ethanol
This research was funded in part by a University of Georgia Graduate Student Assistantship to M.C. Edwards, and the Center for Undergraduate Research Opportunities at the University of Georgia provided partial funding to support T.D. Williams. We thank Alyssa Balles for her assistance with the saccharifications. All authors have agreed to submit this manuscript to the “Journal of Industrial Microbiology and Biotechnology.” Fermentations and characterization of pectinases were partially supported by a grant from the US Department of Energy, Energy Efficiency and Renewable Energy (DE-EE0000410). The glycome profiling was supported by the BioEnergy Science Center administered by Oak Ridge National Laboratory and funded by a grant (DE-AC05-00OR22725) from the Office of Biological and Environmental Research, Office of Science, US Department of Energy. The generation of the CCRC series of plant cell wall glycan-directed monoclonal antibodies used in this work was supported by the NSF Plant Genome Program (DBI-0421683 and IOS-0923992).
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