Abstract
Glycation of whey proteins is primarily affected by temperature, water activity, and pH, and leads to changes of the functional and nutritional properties of the proteins. In the case of prolonged storage of mixtures of lactose and β-lactoglobulin as a model for dried dairy products under mild heat treatment (60–70°C) in a restricted water environment (aw 0.64) at pH 7, Nϵ-(carboxymethyl)lysine (CML) and furosine were formed concomitant with glycation of β-lactoglobulin. Indirect ELISA using polyclonal antibodies against advanced glycation end products (AGEs) was shown to correlate with analyses of CML using HPLC and may be used for quality control of dried dairy products. The glycation changed the solubility properties of the protein by forming polymeric carbohydrate products of β-lactoglobulin and AGEs as characterised by SDS–PAGE.
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