作　　者： ; ; ; ;

机构地区： 华南理工大学轻工与食品学院

出　　处： 《食品科学》 2005年第8期185-188,共4页

摘　　要： 采用商业化的胰蛋白酶对底物浓度为10%的酪朊酸钠进行可控酶解,将酶解液的上清液经截留分子量为10ku的超滤膜分离后利用紫外分光光度法测定各组分ACE体外抑制活性,结果表明酪朊酸钠的胰蛋白酶酶解液具有较强的ACE抑制活性,超滤分离可提高产品的ACE体外抑制活性,为开发新一代降血压保健食品提供广阔的前景。 Sodium caseinate contained peptidic angiotensin I-converting enzyme （ACE） inhibitors, which were released during hydrolysis by trypsin. The molecular mass distributions of the hydrolysates were identified by high performance size exclusion chromatography （HPSEC）. ACE-inhibitory peptides were separated by ultrafiltration in terms of molecular weight. The ACE inhibitory activity of the permeates was IC50=0.42 mg/ml.Ultrafiltration was a effective tool for purification the hydrolysates to obtain thigh ACE-inhibitory activity oeotides.

关 键 词： 酪朊酸钠 胰蛋白酶水解物 高效体积排阻色谱 超滤 抑制肽

领　　域： [轻工技术与工程] [轻工技术与工程]