Solubility of proteins from quail (Coturnix coturnix japonica) egg white as affected by agitation time, pH, and salt concentration
Autor(a) principal: | |
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Data de Publicação: | 2015 |
Outros Autores: | , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | LOCUS Repositório Institucional da UFV |
Texto Completo: | http://dx.doi.org/10.1080/10942912.2012.654557 http://www.locus.ufv.br/handle/123456789/23313 |
Resumo: | The solubility of proteins from quail egg white subjected to different agitation times, pH, and NaCl at 25 ◦ C was evaluated in this study. The greatest solubility achieved was obtained in the 0.05 mol/L of NaCl, pH 10.0, and under agitation for 1 h. The lowest solubility was found in the NaCl 1.0 mol/L, pH 3.0, and agitated for 2 h. Under the test conditions, aqueous solutions of NaCl 1.0 mol/L, pH 3.0, and agitated for 2 h may provide the greatest extraction index of proteins from quail egg white because these conditions promoted the protein precipitation in a large extension. |
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LOCUS Repositório Institucional da UFV |
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spelling |
Santos, D. O.Coimbra, J. S. R.Teixeira, C. R.Barreto, S. L. T.Silva, M. C. H.Giraldo- Zuniga, A. D.2019-02-01T18:12:01Z2019-02-01T18:12:01Z20151532-2386http://dx.doi.org/10.1080/10942912.2012.654557http://www.locus.ufv.br/handle/123456789/23313The solubility of proteins from quail egg white subjected to different agitation times, pH, and NaCl at 25 ◦ C was evaluated in this study. The greatest solubility achieved was obtained in the 0.05 mol/L of NaCl, pH 10.0, and under agitation for 1 h. The lowest solubility was found in the NaCl 1.0 mol/L, pH 3.0, and agitated for 2 h. Under the test conditions, aqueous solutions of NaCl 1.0 mol/L, pH 3.0, and agitated for 2 h may provide the greatest extraction index of proteins from quail egg white because these conditions promoted the protein precipitation in a large extension.engInternational Journal of Food PropertiesVolume 18, Issue 2, Pages 250- 258, 2015SolubilityEggProteinFunctional propertiesPhSolubility of proteins from quail (Coturnix coturnix japonica) egg white as affected by agitation time, pH, and salt concentrationinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfinfo:eu-repo/semantics/openAccessreponame:LOCUS Repositório Institucional da UFVinstname:Universidade Federal de Viçosa (UFV)instacron:UFVORIGINALartigo.pdfartigo.pdftexto completoapplication/pdf688588https://locus.ufv.br//bitstream/123456789/23313/1/artigo.pdf883c86fe570b9cd3c6b683c437e3abd2MD51LICENSElicense.txtlicense.txttext/plain; charset=utf-81748https://locus.ufv.br//bitstream/123456789/23313/2/license.txt8a4605be74aa9ea9d79846c1fba20a33MD52123456789/233132019-02-01 16:17:32.555oai:locus.ufv.br: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Repositório InstitucionalPUBhttps://www.locus.ufv.br/oai/requestfabiojreis@ufv.bropendoar:21452019-02-01T19:17:32LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV)false |
dc.title.en.fl_str_mv |
Solubility of proteins from quail (Coturnix coturnix japonica) egg white as affected by agitation time, pH, and salt concentration |
title |
Solubility of proteins from quail (Coturnix coturnix japonica) egg white as affected by agitation time, pH, and salt concentration |
spellingShingle |
Solubility of proteins from quail (Coturnix coturnix japonica) egg white as affected by agitation time, pH, and salt concentration Santos, D. O. Solubility Egg Protein Functional properties Ph |
title_short |
Solubility of proteins from quail (Coturnix coturnix japonica) egg white as affected by agitation time, pH, and salt concentration |
title_full |
Solubility of proteins from quail (Coturnix coturnix japonica) egg white as affected by agitation time, pH, and salt concentration |
title_fullStr |
Solubility of proteins from quail (Coturnix coturnix japonica) egg white as affected by agitation time, pH, and salt concentration |
title_full_unstemmed |
Solubility of proteins from quail (Coturnix coturnix japonica) egg white as affected by agitation time, pH, and salt concentration |
title_sort |
Solubility of proteins from quail (Coturnix coturnix japonica) egg white as affected by agitation time, pH, and salt concentration |
author |
Santos, D. O. |
author_facet |
Santos, D. O. Coimbra, J. S. R. Teixeira, C. R. Barreto, S. L. T. Silva, M. C. H. Giraldo- Zuniga, A. D. |
author_role |
author |
author2 |
Coimbra, J. S. R. Teixeira, C. R. Barreto, S. L. T. Silva, M. C. H. Giraldo- Zuniga, A. D. |
author2_role |
author author author author author |
dc.contributor.author.fl_str_mv |
Santos, D. O. Coimbra, J. S. R. Teixeira, C. R. Barreto, S. L. T. Silva, M. C. H. Giraldo- Zuniga, A. D. |
dc.subject.pt-BR.fl_str_mv |
Solubility Egg Protein Functional properties Ph |
topic |
Solubility Egg Protein Functional properties Ph |
description |
The solubility of proteins from quail egg white subjected to different agitation times, pH, and NaCl at 25 ◦ C was evaluated in this study. The greatest solubility achieved was obtained in the 0.05 mol/L of NaCl, pH 10.0, and under agitation for 1 h. The lowest solubility was found in the NaCl 1.0 mol/L, pH 3.0, and agitated for 2 h. Under the test conditions, aqueous solutions of NaCl 1.0 mol/L, pH 3.0, and agitated for 2 h may provide the greatest extraction index of proteins from quail egg white because these conditions promoted the protein precipitation in a large extension. |
publishDate |
2015 |
dc.date.issued.fl_str_mv |
2015 |
dc.date.accessioned.fl_str_mv |
2019-02-01T18:12:01Z |
dc.date.available.fl_str_mv |
2019-02-01T18:12:01Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1080/10942912.2012.654557 http://www.locus.ufv.br/handle/123456789/23313 |
dc.identifier.issn.none.fl_str_mv |
1532-2386 |
identifier_str_mv |
1532-2386 |
url |
http://dx.doi.org/10.1080/10942912.2012.654557 http://www.locus.ufv.br/handle/123456789/23313 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.ispartofseries.pt-BR.fl_str_mv |
Volume 18, Issue 2, Pages 250- 258, 2015 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
International Journal of Food Properties |
publisher.none.fl_str_mv |
International Journal of Food Properties |
dc.source.none.fl_str_mv |
reponame:LOCUS Repositório Institucional da UFV instname:Universidade Federal de Viçosa (UFV) instacron:UFV |
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Universidade Federal de Viçosa (UFV) |
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UFV |
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UFV |
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LOCUS Repositório Institucional da UFV |
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LOCUS Repositório Institucional da UFV |
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