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In Vitro Digestibility of Rapeseed and Bovine Whey Protein Mixtures

Joehnke, Marcel Skejovic, Rehder, Alina, Sørensen, Susanne, Bjergegaard, Charlotte, Sørensen, Jens Christian, Markedal, Keld Ejdrup
Journal of agricultural and food chemistry 2018 v.66 no.3 pp. 711-719
Brassica napus, beta-lactoglobulin, cattle, digestibility, digestible protein, dithiothreitol, food industry, hydrolysis, lactalbumin, pancreatin, pepsin, plant proteins, protein concentrates, protein sources, rapeseed, trypsin inhibitors, whey protein
Partial replacement of animal protein sources with plant proteins is highly relevant for the food industry, but potential effects on protein digestibility need to be established. In this study, the in vitro protein digestibility (IVPD) of four protein sources and their mixtures (50:50 w/w ratio) was investigated using a transient pepsin hydrolysis (1 h) followed by pancreatin (1 h). The protein sources consisted of napin-rich rapeseed (Brassica napus L.) protein concentrates (RPCs; RP1, RP2) prepared in pilot scale and major bovine whey proteins (WPs; α-LA, alpha-lactalbumin; β-LG, beta-lactoglobulin). IVPD of individual protein sources was higher for WPs compared to RPCs. The RP2/β-LG mixture resulted in an unexpected high IVPD equivalent to β-LG protein alone. Protein mixtures containing RP1 showed a new IVPD response type due to the negative influence of a high trypsin inhibitor activity (TIA) level. Improved IVPD of RP1 alone and in protein mixtures was obtained by lowering the TIA level using dithiothreitol (DTT). These results showed that napin-rich protein products prepared by appropriate processing can be combined with specific WPs in mixtures to improve the IVPD.