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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Development of hemicellulolytic enzyme mixtures for plant biomass deconstruction on target biotechnological applications

Full text
Author(s):
Goldbeck, Rosana [1] ; Damasio, Andre R. L. [1] ; Goncalves, Thiago A. [1] ; Machado, Carla B. [1] ; Paixao, Douglas A. A. [1] ; Wolf, Lucia D. [1] ; Mandelli, Fernanda [1] ; Rocha, George J. M. [1] ; Ruller, Roberto [1] ; Squina, Fabio M. [1]
Total Authors: 10
Affiliation:
[1] Brazilian Ctr Res Energy & Mat CNPEM, Brazilian Bioethanol Sci & Technol Lab CTBE, BR-13083970 Campinas, SP - Brazil
Total Affiliations: 1
Document type: Journal article
Source: Applied Microbiology and Biotechnology; v. 98, n. 20, p. 8513-8525, OCT 2014.
Web of Science Citations: 23
Abstract

An essential step in the conversion of lignocellulosic biomass to ethanol and other biorefinery products is conversion of cell wall polysaccharides into fermentable sugars by enzymatic hydrolysis. The objective of the present study was to understand the mode of action of hemicellulolytic enzyme mixtures for pretreated sugarcane bagasse (PSB) deconstruction and wheat arabinoxylan (WA) hydrolysis on target biotechnological applications. In this study, five hemicellulolytic enzymes-two endo-1,4-xylanases (GH10 and GH11), two alpha-L-arabinofuranosidases (GH51 and GH54), and one beta-xylosidase (GH43)-were submitted to combinatorial assays using the experimental design strategy, in order to analyze synergistic and antagonistic effects of enzyme interactions on biomass degradation. The xylooligosaccharides (XOSs) released from hydrolysis were analyzed by capillary electrophoresis and quantified by high-performance anion exchange chromatography with pulsed amperometric detection (HPAEC-PAD). Based on this analysis, it was possible to define which enzymatic combinations favor xylose (X1) or XOS production and thus enable the development of target biotechnological applications. Our results demonstrate that if the objective is X1 production from WA, the best enzymatic combination is GH11 + GH54 + GH43, and for xylobiose (X2) production from WA, it is best to combine GH11 + GH51. However, if the goal is to produce XOS, the five enzymes used in WA hydrolysis are important, but for PSB hydrolysis, only GH11 is sufficient. If the final objective is bioethanol production, GH11 is responsible for hydrolyzing 64.3 % of hemicellulose from PSB. This work provides a basis for further studies on enzymatic mechanisms for XOS production, and the development of more efficient and less expensive enzymatic mixtures, targeting commercially viable lignocellulosic ethanol production and other biorefinery products. (AU)

FAPESP's process: 13/18910-3 - Secretion of heterologous glycoproteins in Aspergillus: effect of glycosylation pattern in functional parameters of glycosyl hydrolases
Grantee:André Ricardo de Lima Damasio
Support Opportunities: Scholarships in Brazil - BIOEN - Young Researchers
FAPESP's process: 08/58037-9 - Library generation for biomass-conversion enzymes from soil metagenome
Grantee:Fábio Márcio Squina
Support Opportunities: Program for Research on Bioenergy (BIOEN) - Young Investigators Grants
FAPESP's process: 12/18859-5 - Development of enzymatic model for deconstruction of sugarcane bagasse cell wall
Grantee:Rosana Goldbeck Coelho
Support Opportunities: Scholarships in Brazil - Post-Doctoral