篇名 | Inhibition of Angiotensin I - Converting Enzymes by Enzymatic Hydrolysates from Chicken Blood |
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卷期 | 18:6 |
作者 | Huang, Shu-chen 、 Liu, Pei-jou |
頁次 | 458-463 |
關鍵字 | chicken blood 、 hydrolysates 、 angiotensin converting enzyme inhibition 、 MEDLINE 、 Scopus 、 SCIE |
出刊日期 | 201012 |
This study examined the hydrolysis of chicken blood meal on soluble protein content, peptide content, the degree of hydrolysis and the inhibition of the Angiotensin I - Converting Enzyme (ACE). The results showed that soluble protein, peptide content and the degree of hydrolysis of the hydrolysates increased when either hydrolysis time or enzyme concentration increased. Five-hour long hydrolysis, using 10% Alcalase enzyme produced the highest ACE-inhibition activities. Under these conditions, the Alcalase IC50 value at 0.34 mg peptide/mL was significantly lower than that obtained from other combinations of enzyme, concentration and hydrolysis time. Separation of the hydrolysates by ultrafiltration isolated a fraction (F3) of less than 3000 Da molar mass. The F3 fraction performed with an IC50 value of only 0.06 mg peptide/mL. Further separation by FPLC using a Superdex peptide 10/300 GL gel column produced the highest inhibitory efficiency ratio (1071%/mg/mL). These results suggest that chicken blood hydrolysates can potentially be developed as functional food products in the future.