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Inhibitory action of soybean beta-conglycinin hydrolysates on Salmonella typhimurium translocation in Caco-2 epithelial cell monolayers.

Soybean protein hydrolysates are widely used as functional foods as they have antioxidative properties able to enhance immune responses in humans. The alcalase enzymatic hydrolysates of beta-conglycinin were fractionated by ultrafiltration, and two main fractions, SP1 (<10 kDa) and SP2 (10-20 kDa), were obtained. The effects of these two fractions on the growth, development of epithelial cells, and formation of intercellular tight junctions were tested on an in vitro Caco-2 cell culture system. The inhibitory effects of SP1 and SP2 on the penetration of Salmonella typhimurium into Caco-2 epithelial cells were also examined. The results showed that the addition of >0.05 g/L of SP2 improved epithelial cell growth and that a concentration of 0.5 g/L of SP2 increased intercellular tight junction formation, which resulted in increased of transepithelial monolayer resistance (TER) values. Moreover, a lower S. typhimurium count compared to control was obtained when Caco-2 cells were grown in 0.05 and 0.5 g/L of SP2. These results show that beta-conglycinin hydrolysates play an important role in resisting S. typhimurium penetration into intestinal epithelial cells and that high molecular mass peptides (10-20 kDa) were more effective overall than low molecular mass peptides.