Data/hora: 07/06/2024 17:15:11

Biblioteca(s): 	Embrapa Caprinos e Ovinos.	
Data corrente: 	14/10/2016	
Data da última atualização: 	05/04/2019	
Autoria: 	FREITAS, C. D. T. de; LEITE, H. B.; OLIVEIRA, J. P. B.; AMARAL, J. L.; EGITO, A. S. do; VAIRO-CAVALLI, S.; LOBO, M. D. P.; MONTEIRO-MOREIRA, A. C. O.; VAIRO-CAVALLI, S.; RAMOS, M. V.	
Afiliação: 	Cleverson Diniz Teixeira de Freitas, Federal University of Ceara (UFC) - Fortaleza, CE, Brazil; Hugo B. Leite, UFC - Fortaleza, CE, Brazil; João P. B. Oliveira, UFC - Fortaleza, CE, Brazil; Jackson L. Amaral, UFC - Fortaleza, CE, Brazil; ANTONIO SILVIO DO EGITO, CNPC; Sandra Vairo-Cavalli, Faculty of Exact Sciences, Plant Proteins Research Centre (CIProVe), National University of La Plata - La Plata, Argentina; Marina D. P. Lobo, NUBEX - Núcleo de Biologia Experimental, Centro de Ciências da Saúde, Universidade de Fortaleza (UNIFOR) - Fortaleza, CE, Brazil; Ana C. O. Monteiro-Moreira, Faculty of Exact Sciences, Plant Proteins Research Centre (CIProVe), National University of La Plata - La Plata, Argentina; Sandra Vairo-Cavalli, UNIFOR - Fortaleza, CE, Brazil; Márcio V. Ramos, UFC - Fortaleza, CE, Brazil.	
Título: 	Insights into milk-clotting activity of latex peptidases from Calotropis procera and Cryptostegia grandiflora.	
Ano de publicação: 	2016	
Fonte/Imprenta: 	Food Research International, v. 87, p. 50-59, 2016.	
Idioma: 	Inglês	
Conteúdo: 	Abstract: Latex fractions from Calotropis procera, Cryptostegia grandiflora, Plumeria rubra, and Himatanthus drasticus were assayed in order to prospect for new plant peptidases with milk-clotting activities, for use as rennet alternatives. Only C. procera and C. grandiflora latex fractions exhibited proteolytic and milk-clotting activities, which were not affected by high concentrations of NaCl and CaCl2. However, pre-incubation of both samples at 75 °C for 10 min eliminated completely their activities. Both proteolytic fractions were able to hydrolyze k-casein and to produce peptides of 16 kDa, a similar SDS-PAGE profile to commercial chymosin. RP-HPLC and mass spectrometry analyses of the k-casein peptides showed that the peptidases from C. procera or C. grandiflora hydrolyzed k-casein similar to commercial chymosin. The cheeses made with both latex peptidases exhibited yields, dry masses, and soluble proteins similar to cheeses prepared with commercial chymosin. In conclusion, C. procera and C. grandiflora latex peptidases with the ability to coagulate milk can be used as alternatives to commercial animal chymosin in the cheese manufacturing process.	
Palavras-Chave: 	Cheese; Cryptostegia grandiflora; Enzima coagulante; Himatanthus drasticus; Papain-like peptidase; Protease vegetal; Proteases.	
Thesagro: 	Caseína; Coagulação; Coalho; Extrato Vegetal; Protease; Proteólise; Queijo.	
Thesaurus Nal: 	Casein; Chymosin; Plumeria rubra; Rennet.	
Categoria do assunto: 	Q Alimentos e Nutrição Humana	
Registro original: 	Embrapa Caprinos e Ovinos (CNPC)	
Exemplares: 	CNPC - (31736-1) - UPC - AP - PP -  -  -  - DIS