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Registro Completo |
Biblioteca(s): |
Embrapa Caprinos e Ovinos. |
Data corrente: |
26/06/2024 |
Data da última atualização: |
26/06/2024 |
Autoria: |
TRUJILLO, A. J.; MIRANDA, G.; LEBARS, D.; DELACROIX-BUCHET, A. |
Afiliação: |
GUY MIRANDA. |
Título: |
Proteolytic specificity of chymosin on caprine alpha s1-caseins A and F. |
Ano de publicação: |
1998 |
Fonte/Imprenta: |
Journal of Dairy Research, v. 65, n. 2, p. 233-241, May, 1998. |
DOI: |
10.1017/s0022029997002707. |
Idioma: |
Inglês |
Conteúdo: |
Abstract: From hydrolysis experiments carried out on alpha s1-caseins A and F at pH 5.2 in the presence of 30 g NaCl/l, i.e. the conditions encountered in many young goats' cheeses, it was found that minima of 19 and 9 bonds were sensitive to chymosin in variants A and F respectively. Variant A was hydrolysed faster than variant F and the proteolytic pattern (reversed-phase HPLC and polyacrylamide agarose gel electrophoresis) differed between the variants. Hydrolysates from both variants had a number of cleavage sites in common (Leu20-Leu21, Phe23-Ala24 and Phe32-Arg33 in both variants, Leu101-Lys102 and Leu64-Lys65, Leu120-His121 and Leu83-His84, Leu142-Ala143 and Leu105-Ala106, Leu149-Phe150 and Leu112-Phe113, Leu156-Asp157 and Leu119-Asp120, Trp164-Tyr165 and Trp127-Tyr128 in variants A and F respectively), while other bonds were split only in variant A (Leu16-Asn17, Glu18-Asn19, Phe28-Pro29, Ile44-Gly45, Tyr80-Ile81, Gln82-Lys83, Tyr91-Leu92, Tyr94-Leu95, Leu109-Glu110 and Phe179-Ser180). Major cleavage sites appeared to be at Phe23-Val24, Leu142-Ala143 and Trp164-Tyr165 for variant A, and Phe23-Val24 and Leu64-Lys65 for variant F. Cleavage site Phe23-Val24 could be the origin of the first breakdown product from goat alpha s1-caseins A and F visible in polyacrylamide agarose gel electrophoresis. |
Palavras-Chave: |
Peptide fragments. |
Thesaurus Nal: |
AlphaS1-casein; Amino acid sequences; Casein; Cheese milk; Chymosin; Females; Goat cheese; Goats; High performance liquid chromatography; Polyacrylamide gel electrophoresis; Substrate specificity. |
Categoria do assunto: |
-- |
Marc: |
LEADER 02239naa a2200313 a 4500 001 2165145 005 2024-06-26 008 1998 bl uuuu u00u1 u #d 024 7 $a10.1017/s0022029997002707.$2DOI 100 1 $aTRUJILLO, A. J. 245 $aProteolytic specificity of chymosin on caprine alpha s1-caseins A and F.$h[electronic resource] 260 $c1998 520 $aAbstract: From hydrolysis experiments carried out on alpha s1-caseins A and F at pH 5.2 in the presence of 30 g NaCl/l, i.e. the conditions encountered in many young goats' cheeses, it was found that minima of 19 and 9 bonds were sensitive to chymosin in variants A and F respectively. Variant A was hydrolysed faster than variant F and the proteolytic pattern (reversed-phase HPLC and polyacrylamide agarose gel electrophoresis) differed between the variants. Hydrolysates from both variants had a number of cleavage sites in common (Leu20-Leu21, Phe23-Ala24 and Phe32-Arg33 in both variants, Leu101-Lys102 and Leu64-Lys65, Leu120-His121 and Leu83-His84, Leu142-Ala143 and Leu105-Ala106, Leu149-Phe150 and Leu112-Phe113, Leu156-Asp157 and Leu119-Asp120, Trp164-Tyr165 and Trp127-Tyr128 in variants A and F respectively), while other bonds were split only in variant A (Leu16-Asn17, Glu18-Asn19, Phe28-Pro29, Ile44-Gly45, Tyr80-Ile81, Gln82-Lys83, Tyr91-Leu92, Tyr94-Leu95, Leu109-Glu110 and Phe179-Ser180). Major cleavage sites appeared to be at Phe23-Val24, Leu142-Ala143 and Trp164-Tyr165 for variant A, and Phe23-Val24 and Leu64-Lys65 for variant F. Cleavage site Phe23-Val24 could be the origin of the first breakdown product from goat alpha s1-caseins A and F visible in polyacrylamide agarose gel electrophoresis. 650 $aAlphaS1-casein 650 $aAmino acid sequences 650 $aCasein 650 $aCheese milk 650 $aChymosin 650 $aFemales 650 $aGoat cheese 650 $aGoats 650 $aHigh performance liquid chromatography 650 $aPolyacrylamide gel electrophoresis 650 $aSubstrate specificity 653 $aPeptide fragments 700 1 $aMIRANDA, G. 700 1 $aLEBARS, D. 700 1 $aDELACROIX-BUCHET, A. 773 $tJournal of Dairy Research$gv. 65, n. 2, p. 233-241, May, 1998.
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