Abstract
Maillard reaction products (MRPs) were prepared from a casein–glucose reaction and ultrafiltrated to provide six fractions. The high molecular weight glycated proteins (melanoprotein) were further purified with a Sephadex G-75 column. Two fractions were obtained and analysed for their reducing power and Fe 2+ chelating activity. Results obtained from the first fraction, analysed by Fourier transform infrared spectroscopy (FT-IR) indicated that the amide I, II and III bands of casein were changed by the Maillard reaction. The obtained samples were also hydrolysed with pepsin and trypsin in vitro, and the proteolytic hydrolysates were evaluated for their antioxidant activities. Non-hydrolysed melanoproteins exhibited the highest reducing power, but peptic hydrolysates of different MRPs were more efficient in radical-scavenging activity.
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