Title: Inhibition of angiotensin I - Converting enzymes by enzymatic hydrolysates from chicken blood
Abstract: 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.
Publication Year: 2020
Publication Date: 2020-07-14
Language: en
Type: article
Indexed In: ['crossref']
Access and Citation
Cited By Count: 12
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