水解物
二肽基肽酶
IC50型
化学
水解
肽
大豆蛋白
孵化
酶
生物化学
色谱法
食品科学
体外
作者
Alice B. Nongonierma,Richard J. FitzGerald
标识
DOI:10.1007/s13228-015-0039-2
摘要
Food protein hydrolysates contain peptide sequences with dipeptidyl peptidase IV (DPP-IV) inhibitory properties which may find use to improve serum glucose regulation in type 2 diabetics. Four plant protein isolates from hemp (H), pea (P), rice (R) and soy (S) were hydrolysed with three enzyme preparations: Corolase L10 (Cor), Promod 144MG (Prom) and Protamex (Prot). From the 12 hydrolysates generated after 4-h incubation, 7 yielded DPP-IV inhibitory activity <2.0 mg protein equivalent mL−1. Their IC50 values ranged from 0.73 ± 0.11 to 3.54 ± 0.24 mg dry weight (dw) hydrolysate mL−1 for the 4 h P_Prot and 4 h H_Cor hydrolysates, respectively. Simulated gastrointestinal digestion (SGID) of the intact proteins yielded DPP-IV IC50 values between 1.85 ± 0.34 and 4.50 ± 0.55 mg dw hydrolysate mL−1 for the R and H, respectively. The DPP-IV inhibitory potency of the 4 h hydrolysates subjected to SGID (DPP-IV IC50 ranging from 1.00 ± 0.42 to 3.83 ± 0.36 mg dw hydrolysate mL−1 for the SGID of the 4 h S_Prom and 4 h H_Prot, respectively) was generally higher than that of the corresponding intact protein subjected to SGID, with the exception of the SGID of R and that of the 4 h R_Prot hydrolysate which had similar IC50 values (P > 0.05). To our knowledge, this is the first study reporting that H and P protein hydrolysates inhibit DPP-IV in vitro. This study also demonstrates the potential benefit, in some instances, of hydrolysing plant protein substrates prior to oral ingestion with the view of releasing DPP-IV inhibitory peptides.
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