New peptides obtained by hydrolysis of caseins from bovine milk by protease extracted from the latex Jacaratia corumbensis.

Detalhes bibliográficos
Autor(a) principal: ARRUDA, M. S.
Data de Publicação: 2012
Outros Autores: SILVA, F. O., EGITO, A. S. do, SILVA, T. M. S., LIMA FILHO, J. L., PORTO, A. L. F., MOREIRA, K. A.
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.
id EMBR_4471e8b853bc9ab4a4580a9f0759ba11
oai_identifier_str oai:www.alice.cnptia.embrapa.br:doc/939711
network_acronym_str EMBR
network_name_str Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice)
repository_id_str 2154
spelling 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
_version_ 1794503523263578112