Nanocomplex formation between β-lactoglobulin or caseinomacropeptide and green tea polyphenols: Impact on protein gelation and polyphenols antiproliferative activity

The development of milk functional foods including health-promoting green tea polyphenols represents a challenge for the food industry since the formation of protein-polyphenol complexes may affect both protein technological properties and polyphenols biological activity. The present work aimed at t...

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Autores principales: von Staszewski, M., Jara, F.L., Ruiz, A.L.T.G., Jagus, R.J., Carvalho, J.E., Pilosof, A.M.R.
Formato: JOUR
Materias:
Antitumor activity
Gelation
Green tea polyphenols
Interaction
Whey proteins
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_17564646_v4_n4_p800_vonStaszewski
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id todo:paper_17564646_v4_n4_p800_vonStaszewski
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spelling todo:paper_17564646_v4_n4_p800_vonStaszewski2023-10-03T16:32:40Z Nanocomplex formation between β-lactoglobulin or caseinomacropeptide and green tea polyphenols: Impact on protein gelation and polyphenols antiproliferative activity von Staszewski, M. Jara, F.L. Ruiz, A.L.T.G. Jagus, R.J. Carvalho, J.E. Pilosof, A.M.R. Antitumor activity Gelation Green tea polyphenols Interaction Whey proteins The development of milk functional foods including health-promoting green tea polyphenols represents a challenge for the food industry since the formation of protein-polyphenol complexes may affect both protein technological properties and polyphenols biological activity. The present work aimed at the characterization of complexes formed between green tea polyphenols and either β-lactoglobulin (β-lg) or caseinomacropeptide (CMP), as well as to evaluate how this complexation may impact on protein gelation and polyphenol antiproliferative activity against tumor cell lines. Particle size and charge of protein-polyphenol complexes depend on protein nature and pH. At pH 6 they had the smallest size and were soluble. The presence of polyphenols accelerated the gelation of both β-lg and CMP, and mainly affected viscoelasticity of β-lg gels. Polyphenol complexation by proteins did not inhibit its anti-proliferative activity. Moreover, they exerted a better performance on some particular tumor cell lines. © 2012 Elsevier Ltd. Fil:von Staszewski, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Jara, F.L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Jagus, R.J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Pilosof, A.M.R. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_17564646_v4_n4_p800_vonStaszewski
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Antitumor activity
Gelation
Green tea polyphenols
Interaction
Whey proteins
spellingShingle Antitumor activity
Gelation
Green tea polyphenols
Interaction
Whey proteins
von Staszewski, M.
Jara, F.L.
Ruiz, A.L.T.G.
Jagus, R.J.
Carvalho, J.E.
Pilosof, A.M.R.
Nanocomplex formation between β-lactoglobulin or caseinomacropeptide and green tea polyphenols: Impact on protein gelation and polyphenols antiproliferative activity
topic_facet Antitumor activity
Gelation
Green tea polyphenols
Interaction
Whey proteins
description The development of milk functional foods including health-promoting green tea polyphenols represents a challenge for the food industry since the formation of protein-polyphenol complexes may affect both protein technological properties and polyphenols biological activity. The present work aimed at the characterization of complexes formed between green tea polyphenols and either β-lactoglobulin (β-lg) or caseinomacropeptide (CMP), as well as to evaluate how this complexation may impact on protein gelation and polyphenol antiproliferative activity against tumor cell lines. Particle size and charge of protein-polyphenol complexes depend on protein nature and pH. At pH 6 they had the smallest size and were soluble. The presence of polyphenols accelerated the gelation of both β-lg and CMP, and mainly affected viscoelasticity of β-lg gels. Polyphenol complexation by proteins did not inhibit its anti-proliferative activity. Moreover, they exerted a better performance on some particular tumor cell lines. © 2012 Elsevier Ltd.
format JOUR
author von Staszewski, M.
Jara, F.L.
Ruiz, A.L.T.G.
Jagus, R.J.
Carvalho, J.E.
Pilosof, A.M.R.
author_facet von Staszewski, M.
Jara, F.L.
Ruiz, A.L.T.G.
Jagus, R.J.
Carvalho, J.E.
Pilosof, A.M.R.
author_sort von Staszewski, M.
title Nanocomplex formation between β-lactoglobulin or caseinomacropeptide and green tea polyphenols: Impact on protein gelation and polyphenols antiproliferative activity
title_short Nanocomplex formation between β-lactoglobulin or caseinomacropeptide and green tea polyphenols: Impact on protein gelation and polyphenols antiproliferative activity
title_full Nanocomplex formation between β-lactoglobulin or caseinomacropeptide and green tea polyphenols: Impact on protein gelation and polyphenols antiproliferative activity
title_fullStr Nanocomplex formation between β-lactoglobulin or caseinomacropeptide and green tea polyphenols: Impact on protein gelation and polyphenols antiproliferative activity
title_full_unstemmed Nanocomplex formation between β-lactoglobulin or caseinomacropeptide and green tea polyphenols: Impact on protein gelation and polyphenols antiproliferative activity
title_sort nanocomplex formation between β-lactoglobulin or caseinomacropeptide and green tea polyphenols: impact on protein gelation and polyphenols antiproliferative activity
url http://hdl.handle.net/20.500.12110/paper_17564646_v4_n4_p800_vonStaszewski
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