High-solids content enzymatic hydrolysis of hydrothermally pretreated sugarcane bagasse using a laboratory-made enzyme blend and commercial preparations. Issue 10 (October 2016)

• Record Type: Journal Article
• Authors: Sant'Ana da Silva, Ayla; Fernandes de Souza, Marcella; Ballesteros, Ignacio; Manzanares, Paloma; Ballesteros, Mercedes; P. S. Bon, Elba
• Is Part Of: Process biochemistry. Volume 51:Issue 10(2016:Oct.)
• Page Start: 1561
• Page End: 1567
• Publication Date: 2016-10
• Subjects: Sugarcane bagasse -- High-solids enzymatic hydrolysis -- Commercial cellulases -- Trichoderma reesei -- Aspergillus awamori; Biochemical engineering -- Periodicals; Biotechnology -- Periodicals; Biochemistry -- periodicals; Biotechnology -- periodicals; Chemical Engineering -- periodicals; Génie biochimique -- Périodiques; Biotechnologie -- Périodiques; Biochemical engineering; Biotechnology; Periodicals; 660.63
• DOI: 10.1016/j.procbio.2016.07.018
• Languages: English
• ISSNs: 1359-5113

Abstract

Graphical abstract: Highlights: High-solids hydrolysis were done using commercial (CC) and lab-made (LC) cellulases. The biomass-customized CC enzymes were more efficient in high-solids hydrolysis. The LC enzymes promoted faster liquefaction than CC enzymes. CC enzymes would benefit from the fast liquefaction of the LC enzymes. Glucose release from 20% solids supports the feasibility of ethanol distillation. Abstract: The hydrolysis of hydrothermally treated sugarcane bagasse at dry matter (DM) content of 5%, 15%, and 20% using a laboratory-made blend of Trichoderma reesei Rut C-30 and Aspergillus awamori (TrAa) supernatants was compared with that of commercial enzymes: Celluclast-Novozym 188 (Cel188), Cellic CTec2 (CT2), and CT2 blended with HTec2 (CTH2). Although the glucose yields (80–86%) achieved with all the enzymes were similar at 5% DM, CTH2 and CT2 performed better than Cel188 and TrAa at 20% DM, with yields of 72%, 69%, 45%, and 57%, respectively. Noticeably, TrAa promoted faster liquefaction in the early stages of hydrolysis. The superior CT2′s performance at high DM contents might be associated with its improved resistance to end-product inhibition, as this preparation was the least affected in experiments containing initial exogenous glucose. However, the performance of all the enzymes decreased in the presence of exogenous glucose in comparison to experiments without exogenous glucose.