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Sugarcane bagasse hydrolysis enhancement using BSA

By Antonio Carlos Freitas dos Santos

Abstract

Lignocellulose is composed of polysaccharides linked to lignin and other aromatic compounds, making the sugars not readily available to fermentation. This entails that biomass must go through the unit operations of pretreatment and enzyme hydrolysis. Pretreatment opens the structure to allow the enzymes to act on and hydrolyze cellulose and hemicellulose to glucose and/or xylose which in turn are fermented to ethanol. Concomitantly, the enzymes interact with soluble phenols and insoluble solids derived from lignin that inhibit hydrolysis. This leads to high enzyme loadings and higher production costs. Soluble phenols can be eliminated through washing. Insoluble lignin, however, demands another approach. Using bovine serum albumin (BSA) and pretreated sugarcane bagasse, the effect of blocking solid lignin from adsorbing enzymes during hydrolysis after 72 hours was evaluated. Hydrolysis was carried using 6.25 FPU (Cellulase 13P) and 12.5 IU (Novozyme 188) /g solids (10 mg protein/g solids) at pH 4.8 and 50°C. The conversion was generally higher when BSA was present, 51% (±1%) vs 42% (±1%) with 1.5% solids loading and 46% (±1%) vs 40% (±1%) with 8% solids loading. The use of BSA produced an increase in the final conversion (p-value \u3c 0.001), but conversion decreased as loadings increased. This has been observed in multiple other studies and cannot be explained by a single factor. The basis of this phenomenon is being investigated. Initial experiments that adjusted the enzyme preparation to 2.5 FPU/g glucan (10.5 mg protein/g glucan) of Cellic CTEC3 and improved the mixing of the slurry elevated the conversion to 72% (±5%) without BSA and 76% (±10%) with it, at 1% (w/v) solids loading and 73% (±6%) without BSA and 80% (±10%) with it, at 10% (w/v) solids loading

Topics: Biochemistry|Agricultural engineering
Publisher: 'Purdue University (bepress)'
Year: 2016
OAI identifier: oai:docs.lib.purdue.edu:dissertations-19132
Provided by: Purdue E-Pubs
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