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Registro Completo |
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Biblioteca(s): |
Embrapa Caprinos e Ovinos. |
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Data corrente: |
26/06/2024 |
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Data da última atualização: |
26/06/2024 |
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Autoria: |
COOLBEAR, K. P.; ELGAR, D. F.; COOLBEAR, T.; AYERS, J. S. |
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Afiliação: |
KATE P. COOLBEAR; DAVID F. ELGAR; TIM COOLBEAR; JOHN S. AYERS. |
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Título: |
Comparative study of methods for the isolation and purification of bovine kappa-casein and its hydrolysis by chymosin. |
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Ano de publicação: |
1996 |
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Fonte/Imprenta: |
Journal of Dairy Research, v. 63, n. 1, p. 61-71, Feb. 1996. |
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DOI: |
10.1017/s002202990003154x |
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Idioma: |
Inglês |
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Notas: |
Comparative study. |
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Conteúdo: |
Abstract: kappa-Casein was purified from a single batch of whole acid casein (kappa-A variant) using different methods in order to compare their merits in producing a purified material with a carbohydrate and phosphate heterogeneity representative of the whole kappa-casein complement in milk. Ion-exchange methods of purification gave products of higher purity than precipitation techniques involving final purification by ethanol fractionation, but all methods resulted in kappa-caseins of apparently similar heterogeneity and chemical composition. The purified kappa-caseins were hydrolysed with chymosin and the derived macropeptides isolated. These were all virtually identical as determined by reversed-phase chromatography and gel electrophoresis. Some observations on chymosin hydrolysis of kappa-casein were made. In addition to formation of the major para-kappa-casein (Glu1-Phe105) and macropeptide (Met106-Val169), chymosin hydrolysis at pH 6.6 also resulted in two minor para-kappa-caseins with N-termini corresponding to Phe18 and Ser33 of kappa-casein. At pH 5.5 and 4.5 para-kappa-casein was rapidly hydrolysed into at least six fragments, one of which had an N-terminus corresponding to Trp76 of kappa-casein. At pH 6.6, 5.5 and 4.5 the kappa-casein macropeptide was stable to chymosin, but at pH 2.3 it was hydrolysed by chymosin into fragments with N-termini corresponding to Met106, Ile125, Ala138, Val139, Thr145 and Glu147 of kappa-casein. |
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Palavras-Chave: |
Hydrogen-ion concentration; Isolation purification; Peptide fragments. |
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Thesaurus Nal: |
Casein; Cattle; Chymosin; High performance liquid chromatography; Kappa-casein; Metabolism. |
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Categoria do assunto: |
L Ciência Animal e Produtos de Origem Animal |
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Marc: |
LEADER 02355naa a2200289 a 4500
001 2165138
005 2024-06-26
008 1996 bl uuuu u00u1 u #d
024 7 $a10.1017/s002202990003154x$2DOI
100 1 $aCOOLBEAR, K. P.
245 $aComparative study of methods for the isolation and purification of bovine kappa-casein and its hydrolysis by chymosin.$h[electronic resource]
260 $c1996
500 $aComparative study.
520 $aAbstract: kappa-Casein was purified from a single batch of whole acid casein (kappa-A variant) using different methods in order to compare their merits in producing a purified material with a carbohydrate and phosphate heterogeneity representative of the whole kappa-casein complement in milk. Ion-exchange methods of purification gave products of higher purity than precipitation techniques involving final purification by ethanol fractionation, but all methods resulted in kappa-caseins of apparently similar heterogeneity and chemical composition. The purified kappa-caseins were hydrolysed with chymosin and the derived macropeptides isolated. These were all virtually identical as determined by reversed-phase chromatography and gel electrophoresis. Some observations on chymosin hydrolysis of kappa-casein were made. In addition to formation of the major para-kappa-casein (Glu1-Phe105) and macropeptide (Met106-Val169), chymosin hydrolysis at pH 6.6 also resulted in two minor para-kappa-caseins with N-termini corresponding to Phe18 and Ser33 of kappa-casein. At pH 5.5 and 4.5 para-kappa-casein was rapidly hydrolysed into at least six fragments, one of which had an N-terminus corresponding to Trp76 of kappa-casein. At pH 6.6, 5.5 and 4.5 the kappa-casein macropeptide was stable to chymosin, but at pH 2.3 it was hydrolysed by chymosin into fragments with N-termini corresponding to Met106, Ile125, Ala138, Val139, Thr145 and Glu147 of kappa-casein.
650 $aCasein
650 $aCattle
650 $aChymosin
650 $aHigh performance liquid chromatography
650 $aKappa-casein
650 $aMetabolism
653 $aHydrogen-ion concentration
653 $aIsolation purification
653 $aPeptide fragments
700 1 $aELGAR, D. F.
700 1 $aCOOLBEAR, T.
700 1 $aAYERS, J. S.
773 $tJournal of Dairy Research$gv. 63, n. 1, p. 61-71, Feb. 1996.
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| 1. |  | CAIERÃO, E.; PASINATO, A.; PIRES, J. L. F.; PIMENTEL, M. B. M.; HEFLER, E.; LORENZONI, J.; LORO, J. C.; SANDRI, R.; SCHNEIDER, S. Uso de tecnologias em lavouras de trigo no Rio Grande do Sul - safra 2009. In: PIRES, J. L. F.; PASINATO, A.; CAIERAO, E.; TIBOLA, C. S. (Org.). Trigo: resultados de pesquisa - safra 2009. Passo Fundo: Embrapa Trigo, 2010. p. 99-116. (Embrapa Trigo. Documentos, 96).| Tipo: Capítulo em Livro Técnico-Científico |
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