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

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

doi:10.1016/j.febslet.2006.09.039

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

Isabelle Benoit, Michèle Asther, Gerlind Sulzenbacher, Eric Record, Laurence Marmuse, Goetz Parsiegla, Isabelle Gimbert, Marcel Asther, Christophe Bignon

Research output: Contribution to journal/periodical › Article › Scientific › peer-review

56 Citations (Scopus)

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.

Original language	English
Pages (from-to)	5815-21
Number of pages	7
Journal	FEBS Letters
Volume	580
Issue number	25
DOIs	https://doi.org/10.1016/j.febslet.2006.09.039
Publication status	Published - 30 Oct 2006

Keywords

Aspergillus niger
Carboxylic Ester Hydrolases
Catalytic Domain
Circular Dichroism
Crystallography, X-Ray
Enzyme Stability
Escherichia coli
Glycosylation
Models, Molecular
Protein Conformation
Protein Folding
Protein Processing, Post-Translational
Recombinant Proteins
Thermodynamics

Access to Document

10.1016/j.febslet.2006.09.039

Cite this

@article{bf7f22afe58e4c278d3b5370772ac513,

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.",

keywords = "Aspergillus niger, Carboxylic Ester Hydrolases, Catalytic Domain, Circular Dichroism, Crystallography, X-Ray, Enzyme Stability, Escherichia coli, Glycosylation, Models, Molecular, Protein Conformation, Protein Folding, Protein Processing, Post-Translational, Recombinant Proteins, Thermodynamics",

author = "Isabelle Benoit and Mich{\`e}le Asther and Gerlind Sulzenbacher and Eric Record and Laurence Marmuse and Goetz Parsiegla and Isabelle Gimbert and Marcel Asther and Christophe Bignon",

year = "2006",

month = oct,

day = "30",

doi = "10.1016/j.febslet.2006.09.039",

language = "English",

volume = "580",

pages = "5815--21",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "Elsevier B.V.",

number = "25",

}

TY - JOUR

T1 - Respective importance of protein folding and glycosylation in the thermal stability of recombinant feruloyl esterase A

AU - Benoit, Isabelle

AU - Asther, Michèle

AU - Sulzenbacher, Gerlind

AU - Record, Eric

AU - Marmuse, Laurence

AU - Parsiegla, Goetz

AU - Gimbert, Isabelle

AU - Asther, Marcel

AU - Bignon, Christophe

PY - 2006/10/30

Y1 - 2006/10/30

N2 - 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.

AB - 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.

KW - Aspergillus niger

KW - Carboxylic Ester Hydrolases

KW - Catalytic Domain

KW - Circular Dichroism

KW - Crystallography, X-Ray

KW - Enzyme Stability

KW - Escherichia coli

KW - Glycosylation

KW - Models, Molecular

KW - Protein Conformation

KW - Protein Folding

KW - Protein Processing, Post-Translational

KW - Recombinant Proteins

KW - Thermodynamics

U2 - 10.1016/j.febslet.2006.09.039

DO - 10.1016/j.febslet.2006.09.039

M3 - Article

C2 - 17027758

SN - 0014-5793

VL - 580

SP - 5815

EP - 5821

JO - FEBS Letters

JF - FEBS Letters

IS - 25

ER -

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

Abstract

Keywords

Access to Document

Fingerprint

Cite this