Respective importance of protein folding and glycosylation in the thermal stability of recombinant feruloyl esterase A - INRAE - Institut national de recherche pour l’agriculture, l’alimentation et l’environnement Access content directly
Journal Articles FEBS Letters Year : 2006

Respective importance of protein folding and glycosylation in the thermal stability of recombinant feruloyl esterase A

Abstract

The thermal stability of four molecular forms (native, refolded, glycosylated, non-glycosylated) of feruloyl esterase A (FAEA) was studied. From the most to the least thermo-resistant, the four molecular species ranked as follows: (i) glycosylated form produced native, (ii) non-glycosylated form produced native, (iii) non-glycosylated form produced as inclusion bodies and refolded, and (iv) glycosylated form produced native chemically denatured and then refolded. On the basis of these results and of crystal structure data, we discuss the respective importance of protein folding and glycosylation in the thermal stability of recombinant FAEA.

Dates and versions

hal-02668736 , version 1 (31-05-2020)

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Isabelle Benoit, Michèle Asther, Gerlind Sulzenbacher, Eric Record, Laurence Marmuse, et al.. Respective importance of protein folding and glycosylation in the thermal stability of recombinant feruloyl esterase A. FEBS Letters, 2006, 580 (25), pp.5815-5821. ⟨10.1016/j.febslet.2006.09.039⟩. ⟨hal-02668736⟩
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