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Purification and characterization of angiotensin converting enzyme-inhibitory derived from crocodile blood hydrolysates Ciênc. Tecnol. Aliment.
NGO-SON,Arnon; KATEKAEW,Somporn.
Abstract Various enzyme types were used to hydrolyze crocodile blood peptides showing an Angiotensin I-converting enzyme (ACE) inhibitory activity. Alcalase hydrolysates (ALH) and Protease G6 hydrolysates (PG6H) showed the highest degree of hydrolysis (P<0.05). However, PG6H was significantly observed to have an effective ACE-inhibitory (ACE-I) activity (94.23%) with an IC50 of 0.021±0.02 mg/mL. An unbound fraction of PG6H showed the highest ACE-I activity and was then subjected to two steps RP-HPLC process. The potent fractions including RC1 and RC2 exhibiting the highest ACE-I activity (88.33 & 84.54%, respectively) were identified using LC-MS/MS. Two novel ACE-inhibitory peptides were identified as GVAAN (431.25 Da) and LHALLL (679.52 Da), and...
Tipo: Info:eu-repo/semantics/article Palavras-chave: ACE inhibitory peptides; Antihypertension; Crocodile blood hydrolysate.
Ano: 2019 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612019000400818
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