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Bioprospection of pectinase supplementation aimed enzyme cocktails to the degradation of plant biomass

Grant number: 13/14454-3
Support type:Scholarships in Brazil - Post-Doctorate
Effective date (Start): October 01, 2013
Effective date (End): June 30, 2017
Field of knowledge:Biological Sciences - Biochemistry - Enzymology
Principal researcher:Richard John Ward
Grantee:Carla Botelho Machado
Home Institution: Centro Nacional de Pesquisa em Energia e Materiais (CNPEM). Ministério da Ciência, Tecnologia e Inovações (Brasil). Campinas , SP, Brazil
Associated research grant:10/18850-2 - Identification, characterization and engineering of plant cell wall degrading enzymes, AP.TEM
Associated scholarship(s):16/06765-7 - Effects of the pectinolytic activity of pectin methyl esterase-CBM3 chimeras on the saccharification of different biomass feedstocks, BE.EP.PD

Abstract

The biodegradation of lignocellulosic materials has been the subject of many studies, because in addition to match an important step in the carbon cycle in nature, presents a huge potential of biotechnology in the production of biofuels. The conversion of lignocellulosic biomass into renewable fuels, such as bioethanol, has been considered a promising technology to replace fossil fuels and expansion of ethanol production worldwide. An essential step in the conversion of lignocellulosic biomass to ethanol or other products biorefinery is the depolymerization of polysaccharides constituents to fermentable sugars by enzymatic pathway. Accordingly completely hydrolyze biomass depends on the synergistic action of several distinct catalytic activities, mainly cellulases and hemicellulases, with which it hopes to obtain synergistic levels of income for saccharification of these complex polymers. Recent studies show that sugar cane has about 30% cellulose, 50% hemicellulose and 10% pectin subpopulation which is linked to the cell wall phenolics and / or lignin and pectin tightly associated with cellulose. For the hydrolysis of biomass to be more efficient, studies have shown that the addition of a cocktail pectinase is highly promising. On the face of it, this research project aims to explore an arsenal pectinolitic composed of the major pectinases described as endo-polygalacturonase, exo-polygalacturonase rhamnogalacturonase (belonging to family GH28) and accessory enzymes of family GH43 (galactanase and arabinanase) compatible with biochemical characteristics for using enzyme cocktails. The accessory enzymes are of paramount importance for the degradation of pectin side chains present in the cell walls of plants. For that, we propose two different methodologies: first, prospecting in silico to retrieve new pectinases micro-organisms known as decomposers of plant biomass and accessory enzymes. This search will be directed from the search for sequences with homology to a major pectinases available in the market Pectinex XL (Aspergillus niger Novozymes) using database available on line and a second methodology using the bioprospecting of endo-polygalacturonase by adopting a metagenomics strategy optimized. These results will be important to target the best combination of pectinases who shall compose new enzyme cocktails, which may contribute to the increased performance and efficiency in the process of hydrolysis of plant biomass.

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Scientific publications
(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)
MACHADO, CARLA BOTELHO; CITADINI, ANA PAULA; GOLDBECK, ROSANA; DE LIMA, EVANDRO ANTONIO; FIGUEIREDO, FERNANDA LOPES; DA SILVA, TONY MARCIO; HOFFMAM, ZAIRA BRUNA; DE SOUSA, AMANDA SILVA; SQUINA, FABIO MARCIO; TEIXEIRA DE MORAES POLIZELI, MARIA DE LOURDES; et al. Increased biomass saccharification by supplementation of a commercial enzyme cocktail with endo-arabinanase from Bacillus licheniformis. Biotechnology Letters, v. 37, n. 7, p. 1455-1462, . (13/14454-3, 10/18850-2)

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