ANGIOTENSIN I-CONVERTING ENZYME (ACE) INHIBITORY ACTIVITY OF HYDROLYSATES OBTAINED FROM MUSCLE FOOD INDUSTRY BY-PRODUCTS – A SHORT REPORT.
 
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Pol. J. Food Nutr. Sci. 2005;55(2):133–138
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ABSTRACT
Enzymatic hydrolysate (Alcalase catalysed) was obtained from cracklings (CEH) and acid hydrolysates were prepared from cracklings (CAH) and chicken feathers (FAH). The degree of hydrolysis (DH) of CEH, CAH, and FAH were 14.0%, 53.8%, and 46.2%, respectively. The results of the SE-HPLC confirmed that small molecular weight peptides composed a considerable fraction of all hydrolysates. The crude hydrolysates exhibited angiotensin I-converting enzyme (ACE) inhibitory activity as determined using hippuryl-His-Leu as the substrate. The inhibition of ACE by CEH, CAH, and FAH was 72.3%, 50.0%, and 49.6% under identical assay conditions.
ISSN:1230-0322