Enhancing Lipolysis-Stimulating Activity of Potato Protein Hydrolysate Using Limited Enzymatic Hydrolysis and Ultrafiltration

The aim of this study was to explore the lipolysis-stimulating activity of potato protein hydrolysate (PPH) using 3T3-L1 adipocytes. Intracellular triglyceride residue (TR) was employed as a marker for lipolysis in cells. The lower TR represents the better lipolysis-stimulating activity in aipocytes at 100-800 ppm levels. Among 6 enzymes, Alcalase was selected to hydrolyze PPH for 6 h to obtain APPH6h with the lowest TR. The sequential fractionation of APPH6h with 30-1 kDa molecular weight cut-off (MWCO) membranes in order to obtain a 10 kDa retentate resulted in further enhancement of its lipolysis-stimulating activity in the cells. The TR significantly decreased from 6.16 to 5.84 mole/mg protein at the 800 ppm level. According to the MTT test on cell viability, 10 kDa retentate in the range of 25-1600 ppm was not toxic to the adipocytes.