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Electrochemical modifications of proteins: disulfide bonds reduction

Philippe Cayot 1 Hélène Rosier 1 Loïc Roullier 2 Thomas Haertlé 3 Gérard Tainturier 1
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 : Electrochemistry Reduction Protein Disulfide bonds Lysozyme
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Philippe Cayot, Hélène Rosier, Loïc Roullier, Thomas Haertlé, Gérard Tainturier. Electrochemical modifications of proteins: disulfide bonds reduction. Food Chemistry, Elsevier, 2002, pp.309-315. ⟨hal-02146555⟩

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