The Penicillium echinulatum Secretome on Sugar Cane Bagasse

Abstract

Plant feedstocks are at the leading front of the biofuel industry based on the potential to promote economical, social and environmental development worldwide through sustainable scenarios related to energy production. Penicillium echinulatum is a promising strain for the bioethanol industry based on its capacity to produce large amounts of cellulases at low cost. The secretome profile of P. echinulatum after grown on integral sugarcane bagasse, microcrystalline cellulose and three types of pretreated sugarcane bagasse was evaluated using shotgun proteomics. The comprehensive chemical characterization of the biomass used as the source of fungal nutrition, as well as biochemical activity assays using a collection of natural polysaccharides, were also performed. Our study revealed that the enzymatic repertoire of P. echinulatum is geared mainly toward producing enzymes from the cellulose complex (endogluganases, cellobiohydrolases and β-glucosidases). Glycoside hydrolase (GH) family members, important to biomass-to-biofuels conversion strategies, were identified, including endoglucanases GH5, 7, 6, 12, 17 and 61, β-glycosidase GH3, xylanases GH10 and GH11, as well as debranching hemicellulases from GH43, GH62 and CE2 and pectinanes from GH28. Collectively, the approach conducted in this study gave new insights on the better comprehension of the composition and degradation capability of an industrial cellulolytic strain, from which a number of applied technologies, such as biofuel production, can be generated.

First Structural Insights into α-l-Arabinofuranosidases from the Two GH62 Glycoside Hydrolase Subfamilies

“…One ␣-helix is observed in the C-terminal region, which is formed by an extra amino acid resulting from the cloning of the protein. Additionally, a disulfide between Cys 10 and Cys 278 constrains the solvent exposed N-terminal part of the polypeptide chain in the vicinity of the loop connecting strands 18 (residues 260 -264) and 19 (residues 281-287). This loop obstrudes the bottom of the tunnel delineated by the five blades of the ␤-propeller.…”

Genomics Review of Holocellulose Deconstruction by Aspergilli

“…Thus, we considered only GH12 and GH74 XEGs from aspergilli, due to the lack of characterized gene models for the GH5, GH16, and GH44 families. Furthermore, XEGs from these families were not identified in secretomes of aspergilli growing on biomass (10,14,203,204). Table 9 shows that aspergilli contain one or no GH74 xyloglucanases but several GH12 enzymes.…”

Proteomics Insights into the Biomass Hydrolysis Potentials of a Hypercellulolytic Fungus Penicillium funiculosum

“…23 Comprehending the 4 enzymatic apparatus of cellulolytic strains, with a focus on achieving better efficiency thus, is a key biotechnological bottleneck to be overcome before the production of liquid biofuels from lignocellulosic biomass becomes a commercial reality. 24,25 In this regards, the mass spectrometric-based proteomic analysis of the secretome serves as a valuable tool in the discovery of new enzymes or interesting enzyme complexes associated with improved lignocellulose deconstruction. 23,26 While the advances in mass spectrometry based proteomics machines and methods continually aids in elucidating the biological roles of protein players in several biological process, 22 it focuses more on the description of carbohydrate active proteins and accessory components involved in the degradation of plant cell wall polysaccharides in cellulolytic fungi.…”