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Effects of enzyme loading and β-glucosidase supplementation on enzymatic hydrolysis of switchgrass processed by leading pretreatment technologies

The objective of this work is to investigate the effects of cellulase loading and β-glucosidase supplementation on enzymatic hydrolysis of pretreated Dacotah switchgrass. To assess the difference among various pretreatment methods, the profiles of sugars and intermediates were determined for differe...

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Bibliographic Details
Published in:Bioresource technology 2011-12, Vol.102 (24), p.11115-11120
Main Authors: Pallapolu, Venkata Ramesh, Lee, Y.Y., Garlock, Rebecca J., Balan, Venkatesh, Dale, Bruce E., Kim, Youngmi, Mosier, Nathan S., Ladisch, Michael R., Falls, Matthew, Holtzapple, Mark T., Sierra-Ramirez, Rocio, Shi, Jian, Ebrik, Mirvat A., Redmond, Tim, Yang, Bin, Wyman, Charles E., Donohoe, Bryon S., Vinzant, Todd B., Elander, Richard T., Hames, Bonnie, Thomas, Steve, Warner, Ryan E.
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Language:English
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Summary:The objective of this work is to investigate the effects of cellulase loading and β-glucosidase supplementation on enzymatic hydrolysis of pretreated Dacotah switchgrass. To assess the difference among various pretreatment methods, the profiles of sugars and intermediates were determined for differently treated substrates. For all pretreatments, 72 h glucan/xylan digestibilities increased sharply with enzyme loading up to 25 mg protein/g-glucan, after which the response varied depending on the pretreatment method. For a fixed level of enzyme loading, dilute sulfuric acid (DA), SO 2, and Lime pretreatments exhibited higher digestibility than the soaking in aqueous ammonia (SAA) and ammonia fiber expansion (AFEX). Supplementation of Novozyme-188 to Spezyme-CP improved the 72 h glucan digestibility only for the SAA treated samples. The effect of β-glucosidase supplementation was discernible only at the early phase of hydrolysis where accumulation of cellobiose and oligomers is significant. Addition of β-glucosidase increased the xylan digestibility of alkaline treated samples due to the β-xylosidase activity present in Novozyme-188.
ISSN:0960-8524
1873-2976
DOI:10.1016/j.biortech.2011.03.085