Effect Of Hydrolysates From Soybean Conglycinin On Anti-infection Of E.coli And Intestinal Microbial Community In Mice

Soybean storage proteins are composed mainly of two major components, conglycinin and glycinin. Many studies have demonstrated that the enzymatic hydrolysis of conglycinin improved its functional properties and had various physiological activities such as antihyprtensive, immunostimulating and antioxide activities. In our previous studies, we reported use of pepsin to simulate digestion and fermentation in the animal gastrointestinal tract to hydrolyze conglycinin in vitro. It was found that conglycinin was a better raw material for pepsin mediated production of growth-stimulating peptides for bifidobacteria. Many growth inhibitory substances such as casein hydrolysates on pathological E.coli have been investigated. However, the effect of peptides isolated from conglycinin on the growth of E.coli has not yet been studied. Objectives of the present study were three fold: (i) determine the effect of hydrolysates from conglycinin on the growth of E.coli; (ii) elucidate anti-infection effect of hydrolysates from conglycinin on E.coli in mice; (iii) investigate the effect of hydrolysates from conglycinin on intestinal microbial community using PCR-DGGE.1. The effect of hydrolysates from conglycinin on the growth of E.coliConglycinin is one of the components of soybean storage proteins. In most studies, it has been demonstrated that enzymatically hydrolyzed conglycinin have important physiological activities. In this study, we selected common broth and M₉ culture mediums, pepsin-hydrolysate conglycinin (PTC) and HCl-full hydrolysis of conglycinin (HCL-FHC) to detect the effect of hrdrolysates from conglycinin on the growth of E.coli O₁₃₈ by utilizing 96 well cell culture plate double dilution method. The results showed that pepsin-hydrolysate conglycinin could inhibit growth of E.coli O₁₃₈ at nitrogen concentrations more than 520 mg/ L.