本研究目的在利用3T3-L1脂肪細胞探討馬鈴薯蛋白水解物(PPH)的促脂解活性；胞內相對脂肪殘留量 (RTR)被用來作為細胞脂解作用的指標，RTR愈低代表有較佳的促脂解活性。在六種酵素中以Alcalase水解馬 鈴薯蛋白(PP) 6小時所得水解物APPH6h具有最低的RTR。其次APPH6h利用30-1千道爾吞(kilo-daltons; kDa)分子 量限值(Molecular weight cut-off; MWCO)濾膜進行序列區分，所獲得的10 kDa MWCO保留液(retentate)可進一步提 升APPH6h在細胞中的促脂解活性，當10 kDa MWCO retentate使用濃度為800 ppm時其RTR顯著的從88.4%降低至 83.8%。腸胃道蛋白酶對於800 ppm 10 kDa MWCO retentate的促脂解活性沒有顯著的影響( p < 0.05)。根據西方轉 漬分析及免疫染色分析的結果指出，10 kDa MWCO retentate在脂肪細胞中藉由荷爾蒙敏感性脂解酶的磷酸化及 轉位提升其促脂解活性。

The aim of this study was to explore the lipolysis-stimulating activity of potato protein hydrolysate (PPH) using 3T3-L1 adipocytes. Intracellular relative triglyceride residue (RTR) was employed as a marker for lipolysis in the adipocytes. The lower RTR represents the better lipolysis-stimulating activity. Among 6 enzymes, Alcalase was selected to hydrolyze potato protein (PP) for 6 h to obtain APPH6h with the lowest RTR. 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 RTR significantly decreased from 88.4 to 83.8% at the 800 ppm level. Gastrointestinal proteases have no significant effect ( p > 0.05) on the lipolysis-stimulating activity of 10 kDa retentate at 800 ppm level. Based on Western blot analysis and immunostaining assay, 10 kDa retentate promotes lipolysis by phosphorylation and translocation of hormone-sensitive lipase (HSL) in the adipocytes.