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Registro Completo |
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Biblioteca(s): |
Embrapa Caprinos e Ovinos. |
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Data corrente: |
14/11/2012 |
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Data da última atualização: |
19/05/2022 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Autoria: |
ARRUDA, M. S.; SILVA, F. O.; EGITO, A. S. do; SILVA, T. M. S.; LIMA FILHO, J. L.; PORTO, A. L. F.; MOREIRA, K. A. |
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Afiliação: |
M. S. ARRUDA, LIKA/UFPE - Recife, PE.; F. O. SILVA, UFRPE - Recife, PE.; ANTONIO SILVIO DO EGITO, CNPC; T. M. S. SILVA, UFRPE - Recife, PE; J. L. LIMA FILHO, UFPE - Recife, PE; A. L. F. PORTO, UFPE / UFRPE - Recife, PE; K. A. MOREIRA, UFPE / UFRPE - Recife, PE. |
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Título: |
New peptides obtained by hydrolysis of caseins from bovine milk by protease extracted from the latex Jacaratia corumbensis. |
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Ano de publicação: |
2012 |
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Fonte/Imprenta: |
LWT- Food Science and Technology, v. 49, n. 1, p. 73-79, Jun. 2012. |
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Idioma: |
Inglês |
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Conteúdo: |
Abstract: The casein and its hydrolysates have many desirable functional properties, so there is great interest in its use in food and pharmaceutical industries. The hydrolysis of casein by a new protease obtained from latex Jacaratia corumbensis was performed to obtain antimicrobial peptides. Four proteins were visualized by electrophoresis of the enzyme extract of J. corumbensis, a band of molecular weight of approximately 30 kDa with the presence of other bands of low density. The fractions as-CN, b-CN and k-CN, were subjected to hydrolysis for a period of 1 min 24 h, where aliquots were collected and analyzed by SDS-PAGE to the characterization of peptides. The hydrolysates were evaluated for antimicrobial activity by determining the Minimum Inhibitory Concentration (MIC). The hydrolysates obtained at time of 2 h showed antimicrobial activity against microorganisms Enterococcus faecalis, Bacillus subtilis, Escherichia coli, Pseudomonas aeruginosa, Klebsiella pneumoniae and Staphylococcus aureus, indicating that the peptides obtained by hydrolysis of bovine casein by latex extract J. corumbensis showed activity antimicrobial. This fraction was subjected to reverse phase chromatography for puri?cation of peptides and subsequent mass spectrometric evaluation. The peptides were sequenced and evaluated for their antimicrobial potential. |
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Palavras-Chave: |
Antimicrobial properties; Hydrolyzed proteins. |
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Thesagro: |
Bovino; Caseína; Hidrólise; Jacaratia corumbensis; Latex; Leite; Protease. |
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Thesaurus Nal: |
Antimicrobial peptides; Casein; Caseinates; Milk. |
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Categoria do assunto: |
L Ciência Animal e Produtos de Origem Animal |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/70150/1/API-New-peptides.pdf
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Marc: |
LEADER 02353naa a2200349 a 4500
001 1939711
005 2022-05-19
008 2012 bl uuuu u00u1 u #d
100 1 $aARRUDA, M. S.
245 $aNew peptides obtained by hydrolysis of caseins from bovine milk by protease extracted from the latex Jacaratia corumbensis.$h[electronic resource]
260 $c2012
520 $aAbstract: The casein and its hydrolysates have many desirable functional properties, so there is great interest in its use in food and pharmaceutical industries. The hydrolysis of casein by a new protease obtained from latex Jacaratia corumbensis was performed to obtain antimicrobial peptides. Four proteins were visualized by electrophoresis of the enzyme extract of J. corumbensis, a band of molecular weight of approximately 30 kDa with the presence of other bands of low density. The fractions as-CN, b-CN and k-CN, were subjected to hydrolysis for a period of 1 min 24 h, where aliquots were collected and analyzed by SDS-PAGE to the characterization of peptides. The hydrolysates were evaluated for antimicrobial activity by determining the Minimum Inhibitory Concentration (MIC). The hydrolysates obtained at time of 2 h showed antimicrobial activity against microorganisms Enterococcus faecalis, Bacillus subtilis, Escherichia coli, Pseudomonas aeruginosa, Klebsiella pneumoniae and Staphylococcus aureus, indicating that the peptides obtained by hydrolysis of bovine casein by latex extract J. corumbensis showed activity antimicrobial. This fraction was subjected to reverse phase chromatography for puri?cation of peptides and subsequent mass spectrometric evaluation. The peptides were sequenced and evaluated for their antimicrobial potential.
650 $aAntimicrobial peptides
650 $aCasein
650 $aCaseinates
650 $aMilk
650 $aBovino
650 $aCaseína
650 $aHidrólise
650 $aJacaratia corumbensis
650 $aLatex
650 $aLeite
650 $aProtease
653 $aAntimicrobial properties
653 $aHydrolyzed proteins
700 1 $aSILVA, F. O.
700 1 $aEGITO, A. S. do
700 1 $aSILVA, T. M. S.
700 1 $aLIMA FILHO, J. L.
700 1 $aPORTO, A. L. F.
700 1 $aMOREIRA, K. A.
773 $tLWT- Food Science and Technology$gv. 49, n. 1, p. 73-79, Jun. 2012.
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Registro original: |
Embrapa Caprinos e Ovinos (CNPC) |
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| Registros recuperados : 2 | |
| 2. |  | ARRUDA, M. S.; SILVA, F. O.; EGITO, A. S. do; SILVA, T. M. S.; LIMA FILHO, J. L.; PORTO, A. L. F.; MOREIRA, K. A. New peptides obtained by hydrolysis of caseins from bovine milk by protease extracted from the latex Jacaratia corumbensis. LWT- Food Science and Technology, v. 49, n. 1, p. 73-79, Jun. 2012.| Tipo: Artigo em Periódico Indexado | Circulação/Nível: A - 1 |
| Biblioteca(s): Embrapa Caprinos e Ovinos. |
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| Registros recuperados : 2 | |
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