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Registro Completo |
Biblioteca(s): |
Embrapa Agroindústria de Alimentos. |
Data corrente: |
20/09/2017 |
Data da última atualização: |
08/03/2024 |
Tipo da produção científica: |
Artigo em Periódico Indexado |
Autoria: |
SANTOS, M. B.; CARVALHO, C. W. P. de; GARCIA-ROJAS, E. E. |
Afiliação: |
MONIQUE BARRETO SANTOS, UNIVERSIDADE FEDERAL RURAL DO RIO DE JANEIRO; CARLOS WANDERLEI PILER DE CARVALHO, CTAA; EDWIN ELARD GARCIA-ROJAS, UNIVERSIDADE FEDERAL FLUMINENSE. |
Título: |
Heteroprotein complex formation of bovine serum albumin and lysozyme: Structure and thermal stability. |
Ano de publicação: |
2018 |
Fonte/Imprenta: |
Food Hydrocolloids, n. 74, p. 267-274, 2018. |
Idioma: |
Inglês |
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. |
Palavras-Chave: |
Coacervation; Differential scanning; Electrostatic interaction; Globular proteins; Microencapsulating. |
Thesaurus Nal: |
calorimetry. |
Categoria do assunto: |
X Pesquisa, Tecnologia e Engenharia |
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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Embrapa Agroindústria de Alimentos (CTAA) |
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6. | | SANTOS, M. B.; SANTOS, C. H. C. DOS; CARVALHO, M. G. DE; CARVALHO, C. W. P. de; GARCIA-ROJAS, E. E. Physicochemical, thermal and rheological properties of synthesized carboxymethyl tara gum (Caesalpinia spinosa). International Journal of Biological Macromolecules, v. 134, n. 1, p. 595-603, 2019.Tipo: Artigo em Periódico Indexado | Circulação/Nível: A - 1 |
Biblioteca(s): Embrapa Agroindústria de Alimentos. |
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Registros recuperados : 6 | |
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