Separation and Purification of Lipase Inhibitory Peptide fromFermented Milk by Lactobacillus plantarum Q180

摘要

In this study, we separated and purified lipase inhibitory peptide from fermentedmilk by Q180 with the aim of developinga new functional anti-lipase activity yogurt product. 180 was inoculated into 10% reconstituted skimmed milkand incubated at 37°C until the pH of the culture reached pH 4.4. Thelipase activity was measured using porcine pancreatic lipase. The lipaseinhibitory peptides were gradually isolated by ultrafiltration, reversed phasecolumn chromatography (RPC), reversed phase high-performance liquidchromatography (RP-HPLC), and gel permeation high-performance liquidchromatography (GP-HPLC) from the fermented milk by Q180. An ODS-AQ column was used for the RPC, a Vydac C18column for the RP-HPLC, and a Superdex Peptide HR column for the GP-HPLC. Thepeptide was composed of Asp, Thr, Ile, Ser, Ala, and Gln, and the anti-lipaseactivity (IC ) was 2,817 μg/mL.