Structural and biochemical studies of enzymes involved in the degradation of glucuronoarabinoxylan (GAX)

• Grant number: 18/00082-0
• Support Opportunities: Scholarships in Brazil - Scientific Initiation
• Start date: May 01, 2018
• End date: April 30, 2019
• Field of knowledge: Physical Sciences and Mathematics - Physics
• Principal Investigator: Igor Polikarpov
• Grantee: Natalia Gabrielly Pereira dos Santos
• Host Institution: Instituto de Física de São Carlos (IFSC). Universidade de São Paulo (USP). São Carlos , SP, Brazil
• Associated research grant: 15/13684-0 - Structural and functional studies of enzymes that participate in complex carbohydrates synthesis and degradation, AP.TEM

Abstract

Lignocellulosic biomass is an eminent source for obtaining green chemical inputs, renewable materials, prebiotics and also cellulosic ethanol. The use of enzymes, such as cellulases, hemicellulases and lignases, is a more efficient and modern way for the hydrolysis and depolymerization of lignocellulosic biomass. Hemicellulases play an essential role in the hydrolysis of hemicelluloses such as glucuron (arabino) xylose (GAX). Specifically, the arabinofuranosidases have the function of removing branches of arabinose and together with xylanases to promote the depolymerization of xylan. Thus, the objective of this project is to carry out the prospection and functional and structural studies of arabinofuranosidases of the GH51 family, which is a large family of enzymes but still relatively little studied.

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)

DOS SANTOS, NATALIA GABRIELLY PEREIRA; MACIEL, EDVALDO VASCONCELOS SOARES; MEJIA-CARMONA, KAREN; LANCAS, FERNANDO MAURO. Multidimensional capillary liquid chromatography-tandem mass spectrometry for the determination of multiclass pesticides in ``sugarcane spirits{''} (cachacas). ANALYTICAL AND BIOANALYTICAL CHEMISTRY, v. 412, n. 28, SI, p. 7789-7797, NOV 2020. (19/08168-4, 16/18079-0, 18/00082-0)