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

Benoit Isabelle | Zendy; Asther Michèle | Zendy; Sulzenbacher Gerlind | Zendy; Record Eric | Zendy; Marmuse Laurence | Zendy; Parsiegla Goetz | Zendy; Gimbert Isabelle | Zendy; Asther Marcel | Zendy; Big Christophe | Zendy

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

Author(s) -

Benoit Isabelle,

Asther Michèle,

Sulzenbacher Gerlind,

Record Eric,

Marmuse Laurence,

Parsiegla Goetz,

Gimbert Isabelle,

Asther Marcel,

Big Christophe

Publication year - 2006

Publication title -

febs letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.593

H-Index - 257

eISSN - 1873-3468

pISSN - 0014-5793

DOI - 10.1016/j.febslet.2006.09.039

Subject(s) - recombinant dna , glycosylation , protein folding , chemistry , biochemistry , thermal stability , protein stability , folding (dsp implementation) , gene , organic chemistry , electrical engineering , engineering

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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