Inhibition of Angiotensin I-Converting Enzymes by Enzymatic Hydrolysates from Chicken Blood

雞血水解液抑制血管收縮素轉換酶

黃書政(Shu-Chen Huang) ； 劉佩柔(Pei-Jou Liu)

《藥物食品分析》 18卷6期 (2010/12) Pp. 458-463

摘要

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.

關鍵字

雞血 ； 水解液 ； 血管收縮素轉換酶

並列摘要

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.

並列關鍵字

chicken blood ； hydrolysates ； angiotensin converting enzyme inhibition