In vitro digestion characteristics of cereal protein concentrates as assessed using a pepsin-pancreatin digestion model.

An alkaline extraction method has been used in many studies to extract total protein from cereal samples. Wheat bran protein concentrate (WBPC), oat bran protein concentrate (OBPC), and barley protein concentrate (BPC) were prepared by alkaline extraction and isoelectric precipitation to study their functional and nutritional properties. The three protein concentrates were hydrolysed by an in vitro pepsin-pancreatin digestion model. Their digestibility (%) and degree of hydrolysis (DH%) were evaluated, and SDS-PAGE electrophoresis was used to illustrate the protein and peptides patterns. The change of the particle sizes and the release of the essential amino acids was followed during the digestion process. The in vitro digestibility of WBPC, OBPC and BPC was 87.4%, 96.1% and 76.9%, respectively. The DH% of protein concentrates were between 50 and 60%. The change of the particle size distribution values Dv(50) was assumed to be related to protein aggregations during the digestion. The protein fractions were identified and the degradation during the digestion and were analysed by SDS-PAGE; the gels of WBPC and OBPC digestion showed virtually complete degradation whereas the intensive bands of undigested protein were presented for BPC. The generation of the free amino acids and short chain peptides were significantly higher at the end of the intestinal digestion compared to the stages of before and after gastric digestion. Higher content of the deficient amino acids such as lysine and threonine were found comparing to the level of deficient amino acids in cereal grains but does not meet the daily recommended intake.