Electrochemical modifications of proteins: disulfide bonds reduction

Philippe Cayot; Hélène Rosier; Loïc Roullier; Thomas Haertlé; Gérard Tainturier

doi:10.1016/S0308-8146(01)00352-1

Journal articles

Electrochemical modifications of proteins: disulfide bonds reduction

Philippe Cayot ¹ Hélène Rosier ¹ Loïc Roullier ² Thomas Haertlé ^{3, *} Gérard Tainturier ¹

* Corresponding author

1 Laboratoire Ingénierie Moléculaire et Sensorielle de l'Aliment

2 LSEO - Laboratoire de Synthèse et Electrosynthèse Organométalliques

3 Laboratoire d'étude des interactions des molécules alimentaires

Abstract : 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.

Keywords : Protein Reduction Electrochemistry Disulfide bonds Lysozyme

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Journal articles

Domain :

Life Sciences [q-bio] / Food engineering

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Electrochemical modifications of proteins: disulfide bonds reduction

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