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	Provedor de dados Ciênc. Tecnol. Aliment. (2) Autor KATEKAEW,Somporn (2) NGO-SON,Arnon (1) SAE-EAW,Amporn (1) THAWORNCHINSOMBUT,Supawan (1) WACHIRATTANAPONGMETEE,Kwanruedee (1) Palavra-chave ACE inhibitory peptides (1) Alkaline-aided protein hydrolysate (1) Antihypertension (1) Crocodile blood hydrolysate (1) Myofibrillar protein (1) Natural antioxidant (1) Sarcoplasmic protein (1) Tilapia byproducts (1) Mais... Tipo do documento Info:eu-repo/semantics/article (2) Ano 2019 (2) País Brazil (2) Idioma Inglês (2)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 2 Primeira ... 1 ... Última 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 Production factors affecting antioxidant peptides from tilapia processing byproducts Ciênc. Tecnol. Aliment. WACHIRATTANAPONGMETEE,Kwanruedee; KATEKAEW,Somporn; SAE-EAW,Amporn; THAWORNCHINSOMBUT,Supawan. Abstract This research aimed to elucidate significant factors affecting antioxidant capacity of protein hydrolysates from tilapia processing byproducts. Effects of protein type, substrate concentration (0.4-1.2%) and time of hydrolysis (0-60 min) on antioxidant abilities were investigated. Antioxidant activity of the alkaline-aided protein hydrolysate (APH) hydrolyzed by Protease G6 at 1.2% and 60 min hydrolysis was comparable to the control (minced tilapia muscle hydrolysates) and was more effective than the myofibrillar protein and sarcoplasmic protein hydrolysates. Principal component analysis showed that the APH exert their antioxidant capacity by peroxyl radical quenching ability. These findings provide evidence that the APH from fish byproducts can... Tipo: Info:eu-repo/semantics/article Palavras-chave: Tilapia byproducts; Myofibrillar protein; Sarcoplasmic protein; Alkaline-aided protein hydrolysate; Natural antioxidant. Ano: 2019 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612019000100181 Registros recuperados: 2 Primeira ... 1 ... Última

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