In the reported experiments, the authors have investigated how the interaction of an alkylsulphate with a protein modifies the chemical reactivity of its cystine disulphide bonds, either on globular or keratinic proteins; such modification is greatly dependent on two factors: the pH of the treatment and the chain length of the surfactant. The authors suggest that the interaction takes place via ionic and hydrophobic linkage and postulate that a double layer is formed around the protein structure in equilibrium with surfactant micelles. The studies refered to in this paper help to interpretate the mechanism of the process, the properties of the intermediates and open the possiblity of applying the results to processes such as fermentation or extraction of proteins or ionic macromolecules.

Peer reviewed