Analysis of the carbohydrate-binding-module from Fragaria x ananassa α-L-arabinofuranosidase 1

Analysis of the carbohydrate-binding-module from Fragaria x ananassa α-L-arabinofuranosidase 1

Copyright © 2016 Elsevier Masson SAS. All rights reserved.

Bibliographische Detailangaben
Veröffentlicht in:Plant physiology and biochemistry : PPB. - 1991. - 107(2016) vom: 01. Okt., Seite 96-103
1. Verfasser: Sin, I N (VerfasserIn)
Weitere Verfasser: Perini, M A, Martínez, G A, Civello, P M
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2016
Zugriff auf das übergeordnete Werk:Plant physiology and biochemistry : PPB
Schlagworte:Journal Article Carbohydrate binding module (CBM) Cell wall Heterologous expression Homogalacturonans Strawberry α-L-arabinofuranosidas Receptors, Cell Surface Recombinant Proteins saccharide-binding proteins mehr... Glycoside Hydrolases EC 3.2.1.- alpha-N-arabinofuranosidase EC 3.2.1.55
Beschreibung
Zusammenfassung:Copyright © 2016 Elsevier Masson SAS. All rights reserved.
α-L-arabinofuranosidases (EC 3.2.1.55) are enzymes involved in the catabolism of several cell-wall polysaccharides such as pectins and hemicelluloses, catalyzing the hydrolysis of terminal non-reducing α-L-arabinofuranosil residues. Bioinformatic analysis of the aminoacidic sequences of Fragaria x ananassa α-L-arabinofuranosidases predict a putative carbohydrate-binding-module of the family CBM_4_9, associated to a wide range of carbohydrate affinities. In this study, we report the characterization of the binding affinity profile to different cell wall polysaccharides of the putative CBM of α-L-arabinofuranosidase 1 from Fragaria x ananassa (CBM-FaARA1). The sequence encoding for the putative CBM was cloned and expressed in Escherichia coli, and the resultant recombinant protein was purified from inclusion bodies by a Nickel affinity chromatography under denaturing conditions. The refolded recombinant protein was then subjected to binding assays and affinity gel electrophoresis, which indicated its ability to bind cellulose and also high affinity for homogalacturonans
Beschreibung:Date Completed 27.03.2017
Date Revised 30.09.2020
published: Print-Electronic
Citation Status MEDLINE
ISSN:1873-2690
DOI:10.1016/j.plaphy.2016.05.028