Inhibition of angiotensin I - Converting enzymes by enzymatic hydrolysates from chicken blood
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.
Huang, S.-C. and Liu, P.-J.
"Inhibition of angiotensin I - Converting enzymes by enzymatic hydrolysates from chicken blood,"
Journal of Food and Drug Analysis: Vol. 18
, Article 5.
Available at: https://doi.org/10.38212/2224-6614.2239