Respective importance of protein folding and glycosylation in the thermal stability of recombinant feruloyl esterase A
2006
Benoit, Isabelle | Asther, Michèle | Sulzenbacher, Gerlind | Record, Eric | Marmuse, Laurence | Parsiegla, Goetz | Gimbert, Isabelle | Asther, Marcel, M. | Bignon, Christophe | Unité mixte de recherche de biotechnologie des champignons filamenteux ; Université de la Méditerranée - Aix-Marseille 2-Institut National de la Recherche Agronomique (INRA)-Université de Provence - Aix-Marseille 1 | Architecture et fonction des macromolécules biologiques (AFMB) ; Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS) | Centre de Recherches sur les Macromolécules Végétales (CERMAV) ; Université Joseph Fourier - Grenoble 1 (UJF)-Institut de Chimie - CNRS Chimie (INC-CNRS)-Centre National de la Recherche Scientifique (CNRS)
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Show more [+] Less [-]English. 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.
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