New peptides obtained by hydrolysis of caseins from bovine milk by protease extracted from the latex Jacaratia corumbensis.
Autor(a) principal: | |
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Data de Publicação: | 2012 |
Outros Autores: | , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) |
Texto Completo: | http://www.alice.cnptia.embrapa.br/alice/handle/doc/939711 |
Resumo: | 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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New peptides obtained by hydrolysis of caseins from bovine milk by protease extracted from the latex Jacaratia corumbensis.Antimicrobial propertiesHydrolyzed proteinsBovinoLeiteJacaratia corumbensisCaseínaHidróliseProteaseLatexMilkCaseinatesAntimicrobial peptidesCaseinAbstract: 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.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.ARRUDA, M. S.SILVA, F. O.EGITO, A. S. doSILVA, T. M. S.LIMA FILHO, J. L.PORTO, A. L. F.MOREIRA, K. A.2022-05-20T05:00:33Z2022-05-20T05:00:33Z2012-11-142012info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleLWT- Food Science and Technology, v. 49, n. 1, p. 73-79, Jun. 2012.http://www.alice.cnptia.embrapa.br/alice/handle/doc/939711enginfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice)instname:Empresa Brasileira de Pesquisa Agropecuária (Embrapa)instacron:EMBRAPA2022-05-20T05:00:43Zoai:www.alice.cnptia.embrapa.br:doc/939711Repositório InstitucionalPUBhttps://www.alice.cnptia.embrapa.br/oai/requestopendoar:21542022-05-20T05:00:43falseRepositório InstitucionalPUBhttps://www.alice.cnptia.embrapa.br/oai/requestcg-riaa@embrapa.bropendoar:21542022-05-20T05:00:43Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) - Empresa Brasileira de Pesquisa Agropecuária (Embrapa)false |
dc.title.none.fl_str_mv |
New peptides obtained by hydrolysis of caseins from bovine milk by protease extracted from the latex Jacaratia corumbensis. |
title |
New peptides obtained by hydrolysis of caseins from bovine milk by protease extracted from the latex Jacaratia corumbensis. |
spellingShingle |
New peptides obtained by hydrolysis of caseins from bovine milk by protease extracted from the latex Jacaratia corumbensis. ARRUDA, M. S. Antimicrobial properties Hydrolyzed proteins Bovino Leite Jacaratia corumbensis Caseína Hidrólise Protease Latex Milk Caseinates Antimicrobial peptides Casein |
title_short |
New peptides obtained by hydrolysis of caseins from bovine milk by protease extracted from the latex Jacaratia corumbensis. |
title_full |
New peptides obtained by hydrolysis of caseins from bovine milk by protease extracted from the latex Jacaratia corumbensis. |
title_fullStr |
New peptides obtained by hydrolysis of caseins from bovine milk by protease extracted from the latex Jacaratia corumbensis. |
title_full_unstemmed |
New peptides obtained by hydrolysis of caseins from bovine milk by protease extracted from the latex Jacaratia corumbensis. |
title_sort |
New peptides obtained by hydrolysis of caseins from bovine milk by protease extracted from the latex Jacaratia corumbensis. |
author |
ARRUDA, M. S. |
author_facet |
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. |
author_role |
author |
author2 |
SILVA, F. O. EGITO, A. S. do SILVA, T. M. S. LIMA FILHO, J. L. PORTO, A. L. F. MOREIRA, K. A. |
author2_role |
author author author author author author |
dc.contributor.none.fl_str_mv |
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. |
dc.contributor.author.fl_str_mv |
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. |
dc.subject.por.fl_str_mv |
Antimicrobial properties Hydrolyzed proteins Bovino Leite Jacaratia corumbensis Caseína Hidrólise Protease Latex Milk Caseinates Antimicrobial peptides Casein |
topic |
Antimicrobial properties Hydrolyzed proteins Bovino Leite Jacaratia corumbensis Caseína Hidrólise Protease Latex Milk Caseinates Antimicrobial peptides Casein |
description |
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. |
publishDate |
2012 |
dc.date.none.fl_str_mv |
2012-11-14 2012 2022-05-20T05:00:33Z 2022-05-20T05:00:33Z |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/publishedVersion info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
LWT- Food Science and Technology, v. 49, n. 1, p. 73-79, Jun. 2012. http://www.alice.cnptia.embrapa.br/alice/handle/doc/939711 |
identifier_str_mv |
LWT- Food Science and Technology, v. 49, n. 1, p. 73-79, Jun. 2012. |
url |
http://www.alice.cnptia.embrapa.br/alice/handle/doc/939711 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.source.none.fl_str_mv |
reponame:Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) instname:Empresa Brasileira de Pesquisa Agropecuária (Embrapa) instacron:EMBRAPA |
instname_str |
Empresa Brasileira de Pesquisa Agropecuária (Embrapa) |
instacron_str |
EMBRAPA |
institution |
EMBRAPA |
reponame_str |
Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) |
collection |
Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) |
repository.name.fl_str_mv |
Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) - Empresa Brasileira de Pesquisa Agropecuária (Embrapa) |
repository.mail.fl_str_mv |
cg-riaa@embrapa.br |
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1794503523263578112 |