title: 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.
authors.affiliation: UMR 1163 INRA/Universités de Provence et de la Méditerranée, Unité de Biotechnologie des Champignons Filamenteux, IFR86-BAIM, ESIL, 163 avenue de Luminy CP 925, 13288 MARSEILLE cedex 09, France.
authors.forename: Isabelle
authors.initials: I
authors.lastname: Benoit
authors.forename: Michèle
authors.initials: M
authors.lastname: Asther
authors.forename: Gerlind
authors.initials: G
authors.lastname: Sulzenbacher
authors.forename: Eric
authors.initials: E
authors.lastname: Record
authors.forename: Laurence
authors.initials: L
authors.lastname: Marmuse
authors.forename: Goetz
authors.initials: G
authors.lastname: Parsiegla
authors.forename: Isabelle
authors.initials: I
authors.lastname: Gimbert
authors.forename: Marcel
authors.initials: M
authors.lastname: Asther
authors.forename: Christophe
authors.initials: C
authors.lastname: Bignon
mesh_terms: D001234:Aspergillus niger / Q000201:enzymology / Q000235:genetics; D002265:Carboxylic Ester Hydrolases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D020134:Catalytic Domain; D002942:Circular Dichroism; D018360:Crystallography, X-Ray; D004795:Enzyme Stability; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D006031:Glycosylation; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D011499:Protein Processing, Post-Translational; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D013816:Thermodynamics
chemical_list: D011994:Recombinant Proteins; D002265:Carboxylic Ester Hydrolases; C070196:feruloyl esterase