M113 Comparison of the enzymatic convertibility of glycerol- and sulfuric acid-pretreated sugarcane bagasse using different cellulase preparations
Monday, April 27, 2015
Aventine Ballroom ABC/Grand Foyer, Ballroom Level
Dr. Carlos Martín Medina1, Dr. Pavel Volkov2, Dr. Alexandra Rozhkova2, Dr. Jürgen Puls3 and Prof. Arkady Sinitsyn4, (1)Department of Chemistry, Umeĺ University, Umeĺ, Sweden, (2)A.N. Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, Russia, (3)Thünen Institute for Wood Research, Hamburg, Germany, (4)Lomonosov Moscow State University, Moscow, Russia
Three enzyme preparations based on the cellulase complex of Penicillium sp. and three Trichoderma-based commercial preparations were used for evaluating the enzymatic convertibility of cellulose contained in glycerol- and sulfuric acid-pretreated sugarcane bagasse. Initially, the hydrolysis of the bagasse substrates was monitored using a micro-scale method where the volume of the reaction mixture was 2 mL and the substrate concentration was 50 g/L. One of the Trichoderma preparations and the three Penicillium-derived ones displayed higher sugar formation and better cellulose conversion than the other two cellulases. The best performing preparations were used in a further investigation of the effect of the enzyme load. Increasing the load from 2 to 10 mg protein per g substrate improved the cellulose conversion but it did not increase the specific hydrolysis rate. The selected preparations were then assayed at a higher scale (20 mL of reaction mixture with a substrate concentration of 100 g/L). Regardless of the cellulase preparation and the experiment size, glycerol-pretreated bagasse had a better enzymatic convertibility than acid-pretreated bagasse. The Trichoderma-based commercial preparation Cellic CTec3 led to higher hydrolysis rates and conversions than the Penicillium-based laboratory preparations. Among the Penicillium sp. preparations, B1-Xyl PCA displayed rather good potential for hydrolysing acid-pretreated bagasse, and B1-Hist BGL had a comparable performance both in presence as in absence of A. niger b-glucosidase.