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Registro Completo |
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Biblioteca(s): |
Embrapa Clima Temperado. |
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Data corrente: |
06/01/2009 |
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Data da última atualização: |
06/01/2009 |
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Tipo da produção científica: |
Artigo em Anais de Congresso / Nota Técnica |
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Autoria: |
SILVA, S. D. dos A e.; EMYGDIO, B. M.; GUADAGNIN, J. P.; WINKLER, L.; CASAGRANDE JÚNIOR, J. G.; AIRES, R. F.; ÁVILA, D. T. de; ÁVILA, T. T. de. |
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Título: |
Ensaio regional de avaliação de milho crioulo, RS, 2007/08. |
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Ano de publicação: |
2008 |
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Fonte/Imprenta: |
In: REUNIÃO TÉCNICA ANUAL DE MILHO, 53., REUNIÃO TÉCNICA ANUAL DE SORGO, 36., 2008. Pelotas. Atas e resumos... Pelotas: Embrapa Clima Temperado, 2008. 1 CD-ROM. |
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Idioma: |
Português |
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Categoria do assunto: |
-- |
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Marc: |
LEADER 00669naa a2200193 a 4500
001 1746452
005 2009-01-06
008 2008 bl uuuu u00u1 u #d
100 1 $aSILVA, S. D. dos A e.
245 $aEnsaio regional de avaliação de milho crioulo, RS, 2007/08.
260 $c2008
700 1 $aEMYGDIO, B. M.
700 1 $aGUADAGNIN, J. P.
700 1 $aWINKLER, L.
700 1 $aCASAGRANDE JÚNIOR, J. G.
700 1 $aAIRES, R. F.
700 1 $aÁVILA, D. T. de
700 1 $aÁVILA, T. T. de
773 $tIn: REUNIÃO TÉCNICA ANUAL DE MILHO, 53., REUNIÃO TÉCNICA ANUAL DE SORGO, 36., 2008. Pelotas. Atas e resumos... Pelotas: Embrapa Clima Temperado, 2008. 1 CD-ROM.
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Registro original: |
Embrapa Clima Temperado (CPACT) |
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 | Acesso ao texto completo restrito à biblioteca da Embrapa Agroindústria de Alimentos. Para informações adicionais entre em contato com ctaa.biblioteca@embrapa.br. |
Registro Completo
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Biblioteca(s): |
Embrapa Agroindústria de Alimentos. |
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Data corrente: |
20/09/2017 |
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Data da última atualização: |
08/03/2024 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Circulação/Nível: |
A - 1 |
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Autoria: |
SANTOS, M. B.; CARVALHO, C. W. P. de; GARCIA-ROJAS, E. E. |
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Afiliação: |
MONIQUE BARRETO SANTOS, UNIVERSIDADE FEDERAL RURAL DO RIO DE JANEIRO; CARLOS WANDERLEI PILER DE CARVALHO, CTAA; EDWIN ELARD GARCIA-ROJAS, UNIVERSIDADE FEDERAL FLUMINENSE. |
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Título: |
Heteroprotein complex formation of bovine serum albumin and lysozyme: Structure and thermal stability. |
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Ano de publicação: |
2018 |
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Fonte/Imprenta: |
Food Hydrocolloids, n. 74, p. 267-274, 2018. |
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Idioma: |
Inglês |
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Conteúdo: |
The formation of a heteroprotein complex obtained by the interaction of bovine serum albumin (BSA) and lysozyme (Lys) was investigated by pH variation using turbidimetric analysis and zeta potential (ζ) at different protein ratios and NaCl concentrations. The complexes were formed in a pH range between 8.0 and 11.0, with the ratio r = 0.5 at pH 9.0 presenting the highest complexation. The addition of NaCl decreased the interaction at concentrations of 10 mM. The complex formation occurred between the isoelectric points (pI) of the proteins, close to a balance of charges, mainly by electrostatic interactions with some participation of hydrogen bonds. Differential scanning calorimetry suggested that the interaction gave rise to a new biopolymer due to the formation of a single denaturation point at 67 °C. The structures formed had an average size of ∼1.7 μm, well above that of the isolated proteins, and microscopic analysis revealed that the complexes had a globular structure. BSA/Lys complexes may be a potential bioactive encapsulating agent and may be used as a food ingredient. |
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Palavras-Chave: |
Coacervation; Differential scanning; Electrostatic interaction; Globular proteins; Microencapsulating. |
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Thesaurus NAL: |
calorimetry. |
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Categoria do assunto: |
X Pesquisa, Tecnologia e Engenharia |
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Marc: |
LEADER 01772naa a2200217 a 4500
001 2075911
005 2024-03-08
008 2018 bl uuuu u00u1 u #d
100 1 $aSANTOS, M. B.
245 $aHeteroprotein complex formation of bovine serum albumin and lysozyme$bStructure and thermal stability.$h[electronic resource]
260 $c2018
520 $aThe formation of a heteroprotein complex obtained by the interaction of bovine serum albumin (BSA) and lysozyme (Lys) was investigated by pH variation using turbidimetric analysis and zeta potential (ζ) at different protein ratios and NaCl concentrations. The complexes were formed in a pH range between 8.0 and 11.0, with the ratio r = 0.5 at pH 9.0 presenting the highest complexation. The addition of NaCl decreased the interaction at concentrations of 10 mM. The complex formation occurred between the isoelectric points (pI) of the proteins, close to a balance of charges, mainly by electrostatic interactions with some participation of hydrogen bonds. Differential scanning calorimetry suggested that the interaction gave rise to a new biopolymer due to the formation of a single denaturation point at 67 °C. The structures formed had an average size of ∼1.7 μm, well above that of the isolated proteins, and microscopic analysis revealed that the complexes had a globular structure. BSA/Lys complexes may be a potential bioactive encapsulating agent and may be used as a food ingredient.
650 $acalorimetry
653 $aCoacervation
653 $aDifferential scanning
653 $aElectrostatic interaction
653 $aGlobular proteins
653 $aMicroencapsulating
700 1 $aCARVALHO, C. W. P. de
700 1 $aGARCIA-ROJAS, E. E.
773 $tFood Hydrocolloids$gn. 74, p. 267-274, 2018.
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