Protein Hydrolysate Batch Production with Angiotensin I-Converting Enzyme Inhibitory Activity from Egg Whites

批式製備具ACE活性抑制之卵蛋白胜肽

江文德(Wen-Dee Chiang) ； 李明展(Ming-Jan Lee) ； 郭偉翔(Wei-Shiang Guo) ； 蔡正宗(Tsun-Chung Tsai)

《藥物食品分析》 14卷4期 (2006/12) Pp. 385-390

摘要

運用thermolysin以製備卵蛋白胜肽，經定性並分區以探討各區對ACE活性之抑制，並應用自發性高血壓大鼠(SHR)測試卵蛋白胜肽的抗高血壓功效。在thermolysin最適條件(pH 8及60℃)，及[E]/[S]＝0.02%下，1%粗卵蛋白溶液經水解4小時，離心後澄清液中之產物回收率約80%，此水解物有高度ACE抑制活性(IC(下標 50)＝33 μg/mL)，不具苦味亦無蛋清之腥味，依序經分子量10,000，3,000和1,000 Da膜之超過濾，可提高其濾液對ACE之抑制活性達IC(下標 50)=17 μg/mL。Thermolysin可回收重複使用四次而不降低水解物之ACE活性抑制，SHR實驗顯示口服0.2 g/Kg體重能有效降低高血壓。

關鍵字

血管收縮I-轉化脢 ； 抗高血壓活性 ； 蛋白質水解物 ； 蛋白

並列摘要

Peptides derived from egg whites by thermolysin digestion were fractionated and characterized to investigate their inhibitory activity against angiotensin I-converting enzyme (ACE). The antihypertensive effect of egg white hydrolysates in strain SHR spontaneously hypertensive rats was also investigated. At optimal conditions, pH 8, 60℃, and (E)/(S)=0.02%, digestion of 1% crude egg white solution by thermolysin was carried for 4 hours. The recovery yield from the supernatant after centrifugation was around 80%. The hydrolysate showed high ACE inhibitory activity (IC50=33 μg/mL) and imparted neither bitter taste nor the iron odor of egg whites. Sequential ultra-filtration of hydrolysate with MW cut-off 10,000, 3,000 and 1,000 Da resulted in increased activity from each filtrate up to IC50=17 μg/mL. Thermolysin was recycled from the hydrolysate for subsequent batch use for a total of four batches without reduction in anti-hypertensive activity. The hydrolysate demonstrated an anti-hypertensive activity in spontaneously hypertensive rats at an orally administrated dosage of 0.2 g/kg body weight.

並列關鍵字

angiotensin I-converting enzyme ACE ； antihypertensive activity ； protein hydrolysate ； egg whites