A 1H NMR study of the specificity of α-l-arabinofuranosidases on natural and unnatural substrates - INSA Toulouse - Institut National des Sciences Appliquées de Toulouse Access content directly
Journal Articles Biochimica et Biophysica Acta (BBA) - General Subjects Year : 2014

A 1H NMR study of the specificity of α-l-arabinofuranosidases on natural and unnatural substrates

Abstract

The detailed characterization of arabinoxylan-active enzymes, such as double-substituted xylan arabinofuranosidase activity, is still a challenging topic. Ad hoc chromogenic substrates are useful tools and can reveal subtle differences in enzymatic behavior. In this study, enzyme selectivity on natural substrates has been compared with enzyme selectivity towards aryl-glycosides. This has proven to be a suitable approach to understand how artificial substrates can be used to characterize arabinoxylan-active α-l-arabinofuranosidases (Abfs).
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hal-02146175 , version 1 (03-06-2019)

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Vinciane Borsenberger, Emmie Dornez, Marie-Laure Desrousseaux, Stéphane Massou, Maija Tenkanen, et al.. A 1H NMR study of the specificity of α-l-arabinofuranosidases on natural and unnatural substrates. Biochimica et Biophysica Acta (BBA) - General Subjects, 2014, 1840 (10), pp.3106-3114. ⟨10.1016/j.bbagen.2014.07.001⟩. ⟨hal-02146175⟩
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