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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) - glycosylation , recombinant dna , chemistry , protein folding , biochemistry , thermal stability , native state , esterase , folding (dsp implementation) , n linked glycosylation , enzyme , glycoprotein , organic chemistry , electrical engineering , gene , engineering , glycan
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.