Authors
Camila Ramos Dos Santos, Priscila Oliveira de Giuseppe, Flávio Henrique Moreira de Souza, Letícia Maria Zanphorlin, Mariane Noronha Domingues, Renan Augusto Siqueira Pirolla, Rodrigo Vargas Honorato, Celisa Caldana Costa Tonoli, Mariana Abrahão Bueno de Morais, Vanesa Peixoto de Matos Martins, Lucas Miranda Fonseca, Fernanda Büchli, Paulo Sergio Lopes de Oliveira, Fábio Cesar Gozzo, Mário Tyago Murakami
Publication date
2018/12
Journal
Biotechnology for biofuels
Volume
11
Pages
1-19
Publisher
BioMed Central
Description
Background
Arabinoxylan is an abundant polysaccharide in industrially relevant biomasses such as sugarcane, corn stover and grasses. However, the arabinofuranosyl di-substitutions that decorate the xylan backbone are recalcitrant to most known arabinofuranosidases (Abfs).
Results
In this work, we identified a novel GH51 Abf (XacAbf51) that forms trimers in solution and can cope efficiently with both mono- and di-substitutions at terminal or internal xylopyranosyl units of arabinoxylan. Using mass spectrometry, the kinetic parameters of the hydrolysis of 33-α-l-arabinofuranosyl-xylotetraose and 23,33-di-α-l-arabinofuranosyl-xylotetraose by XacAbf51 were determined, demonstrating the capacity of this enzyme to cleave arabinofuranosyl linkages of internal mono- and di-substituted xylopyranosyl units. Complementation studies of fungal enzyme …
Scholar articles
CR Dos Santos, PO de Giuseppe, FHM de Souza… - Biotechnology for biofuels, 2018