酪朊酸钠制备ACE抑制肽的研究(英文)

Angiotensin-I-converting Enzyme Inhibitory Peptides from Tryptic Hydrolysates of Sodium Caseinate

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.