Home Itens selecionados Provedores de dados OAI Créditos Sobre Ajuda

			Busca avançada
	Provedor de dados Ciênc. Tecnol. Aliment. (2) ArchiMer (1) Autor CHANDRA,Prabir K. (1) Delbarre Ladrat, Christine (1) Fleurence, Joel (1) KATEKAEW,Somporn (1) Noel, Joelle (1) SAE-EAW,Amporn (1) SOBRAL,Paulo J. do A. (1) THAWORNCHINSOMBUT,Supawan (1) Verrez-bagnis, Veronique (1) WACHIRATTANAPONGMETEE,Kwanruedee (1) Mais... Palavra-chave Myofibrillar protein (3) Sarcoplasmic protein (2) Alkaline-aided protein hydrolysate (1) Calpain (1) Dicentrarchus labrax L (1) Edible films (1) Linear viscoelasticity (1) Mechanical properties (1) Natural antioxidant (1) Proteolysis (1) Tilapia byproducts (1) Mais... Tipo do documento Info:eu-repo/semantics/article (2) Text (1) Ano 2019 (1) 2002 (1) 2000 (1) País Brazil (2) France (1) Idioma Inglês (3)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 3 Primeira ... 1 ... Última Calculation of viscoelastic properties of edible films: application of three models Ciênc. Tecnol. Aliment. CHANDRA,Prabir K.; SOBRAL,Paulo J. do A.. The viscoelastic properties of edible films can provide information at the structural level of the biopolymers used. The objective of this work was to test three simple models of linear viscoelastic theory (Maxwell, Generalized Maxwell with two units in parallel, and Burgers) using the results of stress relaxation tests in edible films of myofibrillar proteins of Nile Tilapia. The films were elaborated according to a casting technique and pre-conditioned at 58% relative humidity and 22ºC for 4 days. The testing sample (15mm x 118mm) was submitted to tests of stress relaxation in an equipment of physical measurements, TA.XT2i. The deformation, imposed to the sample, was 1%, guaranteeing the permanency in the domain of the linear viscoelasticity. The models... Tipo: Info:eu-repo/semantics/article Palavras-chave: Edible films; Myofibrillar protein; Linear viscoelasticity; Mechanical properties. Ano: 2000 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612000000200021 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 In vitro proteolysis of myofibrillar and sarcoplasmic proteins of European sea bass (Dicentrarchus Labrax L) by an endogenous m-calpain ArchiMer Verrez-bagnis, Veronique; Delbarre Ladrat, Christine; Noel, Joelle; Fleurence, Joel. The effects of m-calpain isolated from the skeletal muscle of sea bass on sarcoplasmic and myofibrillar proteins isolated from the same tissue were examined in vitro. Incubation of sarcoplasmic proteins with m-calpain resulted in only a slight decrease (0.7 kDa) in the molecular weight (MW) of a 26.5 kDa protein. Degradation of myofibrils, monitored by quantification of TCA-soluble peptides generated, resulted in the maximum amount of peptides being generated after 1 h of incubation at 25degreesC. Noticeable modifications in the SDS-PAGE profile of digested myofibrils were observed, including partial denaturation of myosin heavy chain and the release of tropomyosin, similar to69 and similar to27 kDa doublet bands and a few polypeptides of MW lower than 20... Tipo: Text Palavras-chave: Dicentrarchus labrax L; Proteolysis; Sarcoplasmic protein; Calpain; Myofibrillar protein. Ano: 2002 URL: http://archimer.ifremer.fr/doc/2002/publication-1108.pdf Registros recuperados: 3 Primeira ... 1 ... Última

Empresa Brasileira de Pesquisa Agropecuária - Embrapa Todos os direitos reservados, conforme Lei n° 9.610 Política de Privacidade Área restrita		Embrapa Parque Estação Biológica - PqEB s/n° Brasília, DF - Brasil - CEP 70770-901 Fone: (61) 3448-4433 - Fax: (61) 3448-4890 / 3448-4891 SAC: https://www.embrapa.br/fale-conosco