Solubilityof proteins from quail (Coturnix coturnix japonica) egg white as affected by agitation time, pH, and salt concentration

Detalhes bibliográficos
Autor(a) principal: Santos, D. O.
Data de Publicação: 2015
Outros Autores: Coimbra, J. S. R., Teixeira, C. R., Barreto, S. L. T., Silva, M. C. H., Giraldo- Zuniga, A. D.
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/123456789/22688
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.
id UFV_9f269da4671e71ab7e848cae13b2caa0
oai_identifier_str oai:locus.ufv.br:123456789/22688
network_acronym_str UFV
network_name_str LOCUS Repositório Institucional da UFV
repository_id_str 2145
spelling Santos, D. O.Coimbra, J. S. R.Teixeira, C. R.Barreto, S. L. T.Silva, M. C. H.Giraldo- Zuniga, A. D.2018-12-04T13:11:06Z2018-12-04T13:11:06Z20151532-2386http://dx.doi.org/10.1080/10942912.2012.654557http://www.locus.ufv.br/handle/123456789/22688The 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 propertiespHSolubilityof 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/pdf688590https://locus.ufv.br//bitstream/123456789/22688/1/artigo.pdf3ce872513a954a90b6d8397657b2e9a9MD51LICENSElicense.txtlicense.txttext/plain; charset=utf-81748https://locus.ufv.br//bitstream/123456789/22688/2/license.txt8a4605be74aa9ea9d79846c1fba20a33MD52123456789/226882018-12-04 10:40:06.366oai:locus.ufv.br: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Repositório InstitucionalPUBhttps://www.locus.ufv.br/oai/requestfabiojreis@ufv.bropendoar:21452018-12-04T13:40:06LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV)false
dc.title.en.fl_str_mv Solubilityof proteins from quail (Coturnix coturnix japonica) egg white as affected by agitation time, pH, and salt concentration
title Solubilityof proteins from quail (Coturnix coturnix japonica) egg white as affected by agitation time, pH, and salt concentration
spellingShingle Solubilityof 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 Solubilityof proteins from quail (Coturnix coturnix japonica) egg white as affected by agitation time, pH, and salt concentration
title_full Solubilityof proteins from quail (Coturnix coturnix japonica) egg white as affected by agitation time, pH, and salt concentration
title_fullStr Solubilityof proteins from quail (Coturnix coturnix japonica) egg white as affected by agitation time, pH, and salt concentration
title_full_unstemmed Solubilityof proteins from quail (Coturnix coturnix japonica) egg white as affected by agitation time, pH, and salt concentration
title_sort Solubilityof 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 2018-12-04T13:11:06Z
dc.date.available.fl_str_mv 2018-12-04T13:11:06Z
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/123456789/22688
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/123456789/22688
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
instname_str Universidade Federal de Viçosa (UFV)
instacron_str UFV
institution UFV
reponame_str LOCUS Repositório Institucional da UFV
collection LOCUS Repositório Institucional da UFV
bitstream.url.fl_str_mv https://locus.ufv.br//bitstream/123456789/22688/1/artigo.pdf
https://locus.ufv.br//bitstream/123456789/22688/2/license.txt
bitstream.checksum.fl_str_mv 3ce872513a954a90b6d8397657b2e9a9
8a4605be74aa9ea9d79846c1fba20a33
bitstream.checksumAlgorithm.fl_str_mv MD5
MD5
repository.name.fl_str_mv LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV)
repository.mail.fl_str_mv fabiojreis@ufv.br
_version_ 1801213133341065216

Registros relacionados