| The broad bean protein hydrolysate purified by macroporous adsorption resin was separated and purified by gel filtration chromatography to obtain broad bean protein hydrolysate with cholesterol lowering activity. The results showed that the optimal separation and purification conditions of the broad bean protein hydrolysate by single factor experiment were obtained as follows: with Sep G-10 and G-25 dextran gel as the column filling material, loading amount of 10 mg/mL enzymatic hydrolysate 4 mL, deionized water as mobile phase, elution speed 1 mL/min. After separated and purified by the gel filtration chromatography, the components of F1-F6 six broad bean protein hydrolysates were obtained. Compared with the 10 mg/mL of coletenamine powder positive control, the inhibitory rates of F3 and F6 components to three kinds of cholate salts(sodium cholate, soldium glycocholate, sodium taurocholate) were higher than those of the positive control. The relative inhibition rate of F6 component was the highest, which was (274.98 ± 0.19)%, (140.22 ± 0.20)% and (130.99±0.22)% respectively. |
