Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/62798
Type: Artigo de periódico
Title: Characterization of a Hexameric Exo-Acting GH51 alpha-l-Arabinofuranosidase from the Mesophilic Bacillus subtilis
Author: Hoffmam, ZB
Oliveira, LC
Cota, J
Alvarez, TM
Diogo, JA
Neto, MD
Citadini, APS
Leite, VBP
Squina, FM
Murakami, MT
Ruller, R
Abstract: alpha-l-Arabinofuranosidases (alpha-l-Abfases, EC 3.2.1.55) display a broad specificity against distinct glycosyl moieties in branched hemicellulose and recent studies have demonstrated their synergistic use with cellulases and xylanases for biotechnological processes involving plant biomass degradation. In this study, we examined the structural organization of the arabinofuranosidase (GH51 family) from the mesophilic Bacillus subtilis (AbfA) and its implications on function and stability. The recombinant AbfA showed to be active over a broad temperature range with the maximum activity between 35 and 50 A degrees C, which is desirable for industrial applications. Functional studies demonstrated that AbfA preferentially cleaves debranched or linear arabinan and is an exo-acting enzyme producing arabinose from arabinoheptaose. The enzyme has a canonical circular dichroism spectrum of alpha/beta proteins and exhibits a hexameric quaternary structure in solution, as expected for GH51 members. Thermal denaturation experiments indicated a melting temperature of 53.5 A degrees C, which is in agreement with the temperature-activity curves. The mechanisms associated with the unfolding process were investigated through molecular dynamics simulations evidencing an important contribution of the quaternary arrangement in the stabilization of the beta-sandwich accessory domain and other regions involved in the formation of the catalytic interface of hexameric Abfases belonging to GH51 family.
Subject: Arabinofuranosidase
Glycosyl hydrolase family 51
Bacillus subtilis
Quaternary structure
Country: EUA
Editor: Humana Press Inc
Rights: fechado
Identifier DOI: 10.1007/s12033-013-9677-1
Date Issue: 2013
Appears in Collections:Unicamp - Artigos e Outros Documentos

Files in This Item:
There are no files associated with this item.


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.