Abstract
In this study, hypocholesterolaemic peptides were separated from whey protein trypsin hydrolysates (WPTHs) and the inhibition of cholesterol micellar solubility (ICMS) and the stability of hypocholesterolaemic peptides after exposure to simulated gastrointestinal conditions were evaluated. Whey protein trypsin hydrolysates were concentrated by ultrafiltration and then desalted through macroporous adsorption resin DA201‐C. Sephadex G‐50 gel filtration chromatography was used to separate the hypocholesterolaemic peptides from the fraction eluted with 75% ethanol. The results suggested that the fraction obtained by gel filtration with a molecular weight (MW) ranging from 1900 Da to 3100 Da exhibited the highest hypocholesterolaemic activity. This fraction was further separated by reversed‐phase high‐performance liquid chromatography into 14 fractions; the peptides with the highest activities were obtained from the fifth peak with a MW of 2454 Da and 58.77% ICMS. The hypocholesterolaemic peptides were relatively stable when exposed to simulated gastrointestinal digestion.
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