水解物
豆科植物
体外
受体
化学
生物化学
IC50型
成分
维西林
肽
食品科学
贮藏蛋白
水解
基因
作者
Subhiksha Chandrasekaran,Elvira González de Mejı́a
出处
期刊:Food & Function
[The Royal Society of Chemistry]
日期:2023-01-01
卷期号:14 (18): 8467-8486
被引量:6
摘要
The objective of this study was to evaluate germinated chickpea protein hydrolysate (GCPH) in vitro for its effect on markers of type 2 diabetes (T2D) and bitter taste receptor expression in intestinal epithelial cells. Protein hydrolysate was obtained using ficin, and the resulting peptides were sequenced using LC-ESI-MS/MS. Caco-2 cells were used to determine glucose uptake and extra-oral bitter receptor activation. Three peptides, VVFW, GEAGR, and FDLPAL, were identified in legumin. FDLPAL was the most potent peptide in molecular docking studies with a DPP-IV energy of affinity of -9.8 kcal mol-1. GCPH significantly inhibited DPP-IV production by Caco-2 cells (IC50 = 2.1 mM). Glucose uptake was inhibited in a dose-dependent manner (IC25 = 2.0 mM). A negative correlation was found between glucose uptake and PLCβ2 expression in Caco-2 cells (R value, -0.62). Thus, GCPH has the potential to be commercialized as a functional ingredient.
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