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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. |
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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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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: |
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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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Registro original: |
Embrapa Agroindústria de Alimentos (CTAA) |
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| Registros recuperados : 6 | |
| 3. |  | BUENO, T. V.; FONTES, P. P.; UTIYAMA, A. S.; SANTOS, A. B.; FIETTO, L. G.; MARCELINO-GUIMARÃES, F. C. Characterization of Phapa-6417246 candidate effector: gene model, expression analysis, and computational prediction of its potential targets in soybean. In: ANNUAL MEETING OF THE BRAZILIAN SOCIETY FOR BIOCHEMISTRY AND MOLECULAR BIOLOGY, 52., 2023, Águas de Lindóia. Abstracts... São Paulo: SBBq, 2023.| Tipo: Resumo em Anais de Congresso |
| Biblioteca(s): Embrapa Soja. |
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| 4. | | UTIYAMA, A. S.; ABE, V. Y.; DARBEN, L. M.; CARVALHO, K.; CARVALHO, M. C. C. G. de; MARCELINO-GUIMARÃES, F. C. Avaliação funcional de proteínas candidatas a efetores de Phakopsora pachyrhizi por meio da análise de espécies reativas a oxigênio (ROS) e deposição de calose. In: JORNADA ACADÊMICA DA EMBRAPA SOJA, 13., 2018, Londrina. Resumos expandidos... Londrina: Embrapa Soja, 2018. p. 38-45.| Tipo: Artigo em Anais de Congresso |
| Biblioteca(s): Embrapa Soja. |
|  |
| 5. | | CARVALHO, K.; ABE, V. Y.; DARBEN, L. M.; RINCÃO, M. P.; QI, M.; UTIYAMA, A. S.; CARVALHO, M. C. C. G.; LOPES, I. de O. N.; ABDELNOOR, R. V.; WHITHAM, S. A.; MARCELINO-GUIMARÃES, F. C. Host induced gene silencing in P. pachyrhizi effectors interfere in virulence of soybean attenuating fungal pathogenicity. In: IS-MPMI Congress, 18., 2019, Glasgow. [Abstracts...]. [S. l.: s. n.], 2019.| Tipo: Resumo em Anais de Congresso |
| Biblioteca(s): Embrapa Soja. |
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| 6. | | BUENO, T. V.; FONTES, P. P.; ABE, V. Y.; UTIYAMA, A. S.; SENRA, R. L.; OLIVEIRA, L. S.; SANTOS, A. B. dos; FERREIRA, E. G. C.; DARBEN, L. M.; OLIVEIRA, A. B. de; ABDELNOOR, R. V.; WHITHAM, S. A.; FIETTO, L. G.; MARCELINO-GUIMARÃES, F. C. A Phakopsora pachyrhizi Effector Suppresses PAMP-Triggered Immunity and Interacts with a Soybean Glucan Endo-1,3-β-Glucosidase to Promote Virulence. MOLECULAR PLANT-MICROBE INTERACTIONS, v. 35, n. 9, p. 779-790, 2022.| Tipo: Artigo em Periódico Indexado | Circulação/Nível: A - 1 |
| Biblioteca(s): Embrapa Soja. |
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| Registros recuperados : 6 | |
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| Nenhum registro encontrado para a expressão de busca informada. |
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