Department of Life Sciences, University of Limerick, Castletroy, Limerick, Ireland.
Department of Life Sciences, University of Limerick, Castletroy, Limerick, Ireland; Food for Health Ireland, Department of Life Sciences, University of Limerick, Castletroy, Limerick, Ireland.
Food Chem. 2015 Jun 1;176:64-71. doi: 10.1016/j.foodchem.2014.12.027. Epub 2014 Dec 17.
An alkaline extracted brewers' spent grain protein-enriched isolate (BSG-PI) was hydrolysed using Alcalase, Corolase PP, Flavourzyme and Promod 144MG, yielding Alc hydrolysate (H), CorH, FlavH and ProH, respectively. The degree of hydrolysis (DH) of the protein hydrolysates varied from 4.45% for ProH to 16.4% for CorH. The in vitro ACE inhibitory activity of the BSG-PI increased significantly following 15min incubations with Alcalase, Corolase PP and Flavourzyme. The 5kDa ultrafiltration permeates of FlavH and CorH resulted in lower ACE IC50 values than their respective hydrolysates. The bioactivity of the BSG-PI hydrolysates was retained after simulated gastrointestinal digestion (SGID) while SGID also resulted in the release of ACE inhibitory peptides from the BSG-PI and ProH. UPLC-MS/MS analysis resulted in the identification of 34 peptides. Of 12 synthesised peptides, IVY and ILDL were the most potent, having ACE IC50 values at 80.4±11.9 and 96.4±8.36μM, respectively.
一种碱性提取的啤酒糟蛋白浓缩物（BSG-PI）分别使用碱性蛋白酶（Alcalase）、中性蛋白酶（Corolase PP）、风味蛋白酶（Flavourzyme）和木瓜蛋白酶（Promod 144MG）进行水解，分别得到 Alc 水解产物（H）、CorH、FlavH 和 ProH。这些蛋白水解产物的水解度（DH）范围为 4.45%（ProH）至 16.4%（CorH）。BSG-PI 与 Alcalase、Corolase PP 和 Flavourzyme 孵育 15min 后，其血管紧张素转换酶（ACE）抑制活性显著增加。FlavH 和 CorH 的 5kDa 超滤渗透物的 ACE IC50 值低于其各自的水解产物。BSG-PI 水解产物的生物活性在模拟胃肠道消化（SGID）后得以保留，而 SGID 也从 BSG-PI 和 ProH 中释放出 ACE 抑制肽。UPLC-MS/MS 分析鉴定出 34 种肽。在 12 种合成肽中，IVY 和 ILDL 的抑制活性最强，ACE IC50 值分别为 80.4±11.9μM 和 96.4±8.36μM。
