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| Registros recuperados : 6 | |
| 3. |  | OTONI, C. G.; CARVALHO, A.; CARDOSO, M.; BERNARDINELLI, O.; LOREVICE, M.; COLNAGO, L. A.; LOH, W.; MATTOSO, L. H. C. High-pressure microfluidization as a green tool for optimizing the mechanical performance of all-cellulose composites. ACS Sustainable Chemistry e Engineering, v. 6, n. 10, p. 12727-12735, 21 ago. 2018. 12727-12735| Biblioteca(s): Embrapa Instrumentação. |
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| 4. | | OTONI, C. G.; CARVALHO, A. S.; CARDOSO, M. V. C.; BERNARDINELLI, O. D.; LOREVICE, M. V.; LOH, W. High-pressure microfluidization as a green tool for optimizing the mechanical performance of all-cellulose composites. ACS Sustainable Chemistry & Engineering, [S. l], n. 6, p. 12727-12735, 2018.| Biblioteca(s): Embrapa Instrumentação. |
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| 5. | | WIESMAN, Z.; LINDER, C.; RESENDE, M. T.; AYALON, N.; LEVI, O.; BERNARDINELLI, O. D.; COLNAGO, L. A.; MITRE, C. I. N.; JACKMAN, R. 2D and 3D spectrum graphics of the chemical-morphological domains of complex biomass by low field proton NMR energy relaxation signal analysis. Energy & Fuels, v. 32, n. 4, 2018. 5090-5102| Biblioteca(s): Embrapa Instrumentação. |
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| 6. | | LIMA, M. A.; GOMEZ, L. D.; STEELI-KING, C. G.; SIMISTER, R.; BERNARDINELLI, O. D.; CARVALHO, M. A.; REZENDE, C. A.; LABATE, C. A.; AZEVEDO, E. R.; McQUEEN-MASON, S.; POLIKARPOV, I.; CARVALHO, M. A. Evaluating the composition and processing potential of novel sources of Brazilian biomass for sustainable biorenewables production. Biotechnology for Biofuels, v. 7, n. 10, 2014.| Biblioteca(s): Embrapa Cerrados. |
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 | Acesso ao texto completo restrito à biblioteca da Embrapa Caprinos e Ovinos. Para informações adicionais entre em contato com cnpc.biblioteca@embrapa.br. |
Registro Completo
|
Biblioteca(s): |
Embrapa Caprinos e Ovinos. |
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Data corrente: |
14/10/2016 |
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Data da última atualização: |
05/04/2019 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Circulação/Nível: |
A - 1 |
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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. |
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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. |
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Título: |
Insights into milk-clotting activity of latex peptidases from Calotropis procera and Cryptostegia grandiflora. |
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Ano de publicação: |
2016 |
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Fonte/Imprenta: |
Food Research International, v. 87, p. 50-59, 2016. |
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Idioma: |
Inglês |
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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. |
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Palavras-Chave: |
Cheese; Cryptostegia grandiflora; Enzima coagulante; Himatanthus drasticus; Papain-like peptidase; Protease vegetal; Proteases. |
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Thesagro: |
Caseína; Coagulação; Coalho; Extrato Vegetal; Protease; Proteólise; Queijo. |
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Thesaurus NAL: |
Casein; Chymosin; Plumeria rubra; Rennet. |
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Categoria do assunto: |
Q Alimentos e Nutrição Humana |
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Marc: |
LEADER 02382naa a2200445 a 4500
001 2054705
005 2019-04-05
008 2016 bl uuuu u00u1 u #d
100 1 $aFREITAS, C. D. T. de
245 $aInsights into milk-clotting activity of latex peptidases from Calotropis procera and Cryptostegia grandiflora.
260 $c2016
520 $aAbstract: 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.
650 $aCasein
650 $aChymosin
650 $aPlumeria rubra
650 $aRennet
650 $aCaseína
650 $aCoagulação
650 $aCoalho
650 $aExtrato Vegetal
650 $aProtease
650 $aProteólise
650 $aQueijo
653 $aCheese
653 $aCryptostegia grandiflora
653 $aEnzima coagulante
653 $aHimatanthus drasticus
653 $aPapain-like peptidase
653 $aProtease vegetal
653 $aProteases
700 1 $aLEITE, H. B.
700 1 $aOLIVEIRA, J. P. B.
700 1 $aAMARAL, J. L.
700 1 $aEGITO, A. S. do
700 1 $aVAIRO-CAVALLI, S.
700 1 $aLOBO, M. D. P.
700 1 $aMONTEIRO-MOREIRA, A. C. O.
700 1 $aVAIRO-CAVALLI, S.
700 1 $aRAMOS, M. V.
773 $tFood Research International$gv. 87, p. 50-59, 2016.
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