Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/74685
Type: Artigo de periódico
Title: Substrate cleavage pattern, biophysical characterization and low-resolution structure of a novel hyperthermostable arabinanase from Thermotoga petrophila
Author: Squina, FM
Santos, CR
Ribeiro, DA
Cota, J
de Oliveira, RR
Ruller, R
Mort, A
Murakami, MT
Prade, RA
Abstract: Arabinan is a plant structural polysaccharide degraded by two enzymes: alpha-L-arabinofuranosidase and endo-1,5-alpha-L-arabinanase. These enzymes are highly diversified in nature, however, little is known about their biochemical and biophysical properties. We have characterized a novel arabinanase (AbnA) isolated from Thermotoga petrophila with unique thermostable properties such as the insignificant decrease of residual activity after incubation up to 90 degrees C. We determined the AbnA mode of operation through capillary zone electrophoresis, which accumulates arabinotriose and arabinobiose as end products after hydrolysis of arabinan-containing polysaccharides. Spectroscopic analyses by Far-UV circular dichroism and intrinsic tryptophan fluorescence emission demonstrated that AbnA is folded and formed mainly by beta-sheet structural elements. In silico molecular modeling showed that the AbnA structure encompasses a five-bladed beta-propeller catalytic core juxtaposed by distorted up-and-down beta-barrel domain. The low-resolution structure determined by small angle X-ray scattering indicated that AbnA is monomeric in solution and its molecular shape is in full agreement with the model. (C) 2010 Elsevier Inc. All rights reserved.
Subject: Arabinanase
Capillary zone electrophoresis
Small angle X-ray scattering (SAXS)
Hyperthermostable enzyme
Arabinan
Country: EUA
Editor: Academic Press Inc Elsevier Science
Rights: fechado
Identifier DOI: 10.1016/j.bbrc.2010.07.097
Date Issue: 2010
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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