Production, characterization and foamability of α-lactalbumin/glycomacropeptide supramolecular structures
Autor(a) principal: | |
---|---|
Data de Publicação: | 2014 |
Outros Autores: | , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | LOCUS Repositório Institucional da UFV |
Texto Completo: | http://dx.doi.org/10.1016/j.foodres.2014.05.079 http://www.locus.ufv.br/handle/123456789/22426 |
Resumo: | The study of protein interactions has generated great interest in the food industry. Therefore, research on new supramolecular structures shows promise. Supramolecular structures of the whey proteins α-lactalbumin and glycomacropeptide were produced under varying heat treatments (25 to 75 °C) and acidic conditions (pH 3.5to 6.5). Isothermal titration calorimetry experiments showed protein interactions and demonstrated that this is an enthalpically driven process. Supramolecular protein structures in aqueous solutions were characterized by circular dichroism and intrinsic fluorescence spectroscopy. Additional photon correlation spectroscopy experiments showed that the size distribution of the structures ranged from 4 to 3545 nm among the different conditions. At higher temperatures, lower pH increased particle size. The foamability of the supramolecular protein structures was evaluated. Analysis of variance and analysis of regression for foaming properties indicated that the two-factor interactions between pH and temperature exhibited a significant effect on the volume and stability of the foam. |
id |
UFV_30208a48be6510f343cf284c963b8a2e |
---|---|
oai_identifier_str |
oai:locus.ufv.br:123456789/22426 |
network_acronym_str |
UFV |
network_name_str |
LOCUS Repositório Institucional da UFV |
repository_id_str |
2145 |
spelling |
Diniz, Renata SilvaCoimbra, Jane Sélia dos ReisTeixeira, Álvaro Vianna Novaes de CarvalhoCosta, Angélica Ribeiro daSantos, Igor José BoggioneBressan, Gustavo CostaRodrigues, Antonio Manuel da CruzSilva, Luiza Helena Meller da2018-10-31T10:43:54Z2018-10-31T10:43:54Z2014-06-170963-9969http://dx.doi.org/10.1016/j.foodres.2014.05.079http://www.locus.ufv.br/handle/123456789/22426The study of protein interactions has generated great interest in the food industry. Therefore, research on new supramolecular structures shows promise. Supramolecular structures of the whey proteins α-lactalbumin and glycomacropeptide were produced under varying heat treatments (25 to 75 °C) and acidic conditions (pH 3.5to 6.5). Isothermal titration calorimetry experiments showed protein interactions and demonstrated that this is an enthalpically driven process. Supramolecular protein structures in aqueous solutions were characterized by circular dichroism and intrinsic fluorescence spectroscopy. Additional photon correlation spectroscopy experiments showed that the size distribution of the structures ranged from 4 to 3545 nm among the different conditions. At higher temperatures, lower pH increased particle size. The foamability of the supramolecular protein structures was evaluated. Analysis of variance and analysis of regression for foaming properties indicated that the two-factor interactions between pH and temperature exhibited a significant effect on the volume and stability of the foam.engFood Research Internationalv. 64, p. 157– 165, out. 2014Self-assemblyHeating AcidificationTechno-functional propertiesCalorimetryProduction, characterization and foamability of α-lactalbumin/glycomacropeptide supramolecular structuresinfo: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.pdfartigoapplication/pdf784031https://locus.ufv.br//bitstream/123456789/22426/1/artigo.pdf3e2467dea34f284d46a0bf033e5a2a01MD51LICENSElicense.txtlicense.txttext/plain; charset=utf-81748https://locus.ufv.br//bitstream/123456789/22426/2/license.txt8a4605be74aa9ea9d79846c1fba20a33MD52123456789/224262018-10-31 07:46:58.649oai:locus.ufv.br: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Repositório InstitucionalPUBhttps://www.locus.ufv.br/oai/requestfabiojreis@ufv.bropendoar:21452018-10-31T10:46:58LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV)false |
dc.title.en.fl_str_mv |
Production, characterization and foamability of α-lactalbumin/glycomacropeptide supramolecular structures |
title |
Production, characterization and foamability of α-lactalbumin/glycomacropeptide supramolecular structures |
spellingShingle |
Production, characterization and foamability of α-lactalbumin/glycomacropeptide supramolecular structures Diniz, Renata Silva Self-assembly Heating Acidification Techno-functional properties Calorimetry |
title_short |
Production, characterization and foamability of α-lactalbumin/glycomacropeptide supramolecular structures |
title_full |
Production, characterization and foamability of α-lactalbumin/glycomacropeptide supramolecular structures |
title_fullStr |
Production, characterization and foamability of α-lactalbumin/glycomacropeptide supramolecular structures |
title_full_unstemmed |
Production, characterization and foamability of α-lactalbumin/glycomacropeptide supramolecular structures |
title_sort |
Production, characterization and foamability of α-lactalbumin/glycomacropeptide supramolecular structures |
author |
Diniz, Renata Silva |
author_facet |
Diniz, Renata Silva Coimbra, Jane Sélia dos Reis Teixeira, Álvaro Vianna Novaes de Carvalho Costa, Angélica Ribeiro da Santos, Igor José Boggione Bressan, Gustavo Costa Rodrigues, Antonio Manuel da Cruz Silva, Luiza Helena Meller da |
author_role |
author |
author2 |
Coimbra, Jane Sélia dos Reis Teixeira, Álvaro Vianna Novaes de Carvalho Costa, Angélica Ribeiro da Santos, Igor José Boggione Bressan, Gustavo Costa Rodrigues, Antonio Manuel da Cruz Silva, Luiza Helena Meller da |
author2_role |
author author author author author author author |
dc.contributor.author.fl_str_mv |
Diniz, Renata Silva Coimbra, Jane Sélia dos Reis Teixeira, Álvaro Vianna Novaes de Carvalho Costa, Angélica Ribeiro da Santos, Igor José Boggione Bressan, Gustavo Costa Rodrigues, Antonio Manuel da Cruz Silva, Luiza Helena Meller da |
dc.subject.pt-BR.fl_str_mv |
Self-assembly Heating Acidification Techno-functional properties Calorimetry |
topic |
Self-assembly Heating Acidification Techno-functional properties Calorimetry |
description |
The study of protein interactions has generated great interest in the food industry. Therefore, research on new supramolecular structures shows promise. Supramolecular structures of the whey proteins α-lactalbumin and glycomacropeptide were produced under varying heat treatments (25 to 75 °C) and acidic conditions (pH 3.5to 6.5). Isothermal titration calorimetry experiments showed protein interactions and demonstrated that this is an enthalpically driven process. Supramolecular protein structures in aqueous solutions were characterized by circular dichroism and intrinsic fluorescence spectroscopy. Additional photon correlation spectroscopy experiments showed that the size distribution of the structures ranged from 4 to 3545 nm among the different conditions. At higher temperatures, lower pH increased particle size. The foamability of the supramolecular protein structures was evaluated. Analysis of variance and analysis of regression for foaming properties indicated that the two-factor interactions between pH and temperature exhibited a significant effect on the volume and stability of the foam. |
publishDate |
2014 |
dc.date.issued.fl_str_mv |
2014-06-17 |
dc.date.accessioned.fl_str_mv |
2018-10-31T10:43:54Z |
dc.date.available.fl_str_mv |
2018-10-31T10:43:54Z |
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/10.1016/j.foodres.2014.05.079 http://www.locus.ufv.br/handle/123456789/22426 |
dc.identifier.issn.none.fl_str_mv |
0963-9969 |
identifier_str_mv |
0963-9969 |
url |
http://dx.doi.org/10.1016/j.foodres.2014.05.079 http://www.locus.ufv.br/handle/123456789/22426 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.ispartofseries.pt-BR.fl_str_mv |
v. 64, p. 157– 165, out. 2014 |
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 |
Food Research International |
publisher.none.fl_str_mv |
Food Research International |
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/123456789/22426/1/artigo.pdf https://locus.ufv.br//bitstream/123456789/22426/2/license.txt |
bitstream.checksum.fl_str_mv |
3e2467dea34f284d46a0bf033e5a2a01 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_ |
1801213131417976832 |