Electrochemical modifications of proteins: disulfide bonds reduction

6533b831fe1ef96bd12984d0

RESEARCH PRODUCT

Electrochemical modifications of proteins: disulfide bonds reduction

Hélène Rosier Philippe Cayot Thomas Haertlé Gérard Tainturier Loı̈c Roullier

subject

030303 biophysics Lysozyme Electrochemistry Cleavage (embryo)01 natural sciences Analytical Chemistry 03 medical and health sciences chemistry.chemical_compound Hydrolysis Polymer chemistry [SDV.IDA]Life Sciences [q-bio]/Food engineering Electrochemistry Organic chemistry Denaturation (biochemistry)Disulfide bonds ComputingMilieux_MISCELLANEOUS Reduction chemistry.chemical_classification 0303 health sciences Protein 010401 analytical chemistry Disulfide bond General Medicine [SDV.IDA] Life Sciences [q-bio]/Food engineering 0104 chemical sciences Enzyme chemistry Yield (chemistry)Lysozyme Food Science

description

International audience; Electrochemical reduction of lysozyme disulfide bonds was achieved at pH between 10 and 11.Below pH 10, no disulfide bond cleavage was observed. At pH higher than 12, the cleavage of disulfide bonds is essentially due to hydrolysis. The addition of denaturant considerably enhanced the performance of the electrochemical device.

year	journal	country	edition	language
2002-06-01

10.1016/s0308-8146(01)00352-1 https://hal-agrosup-dijon.archives-ouvertes.fr/hal-02146555

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