Skim milk protein distribution as a result of very high hydrostatic pressure

This work studies the micellar size and the distribution of caseins, major and minor whey proteins in different fractions of skim milk treated up to 900 MPa for 5 min. Transmission electron microscopy showed that the smallest casein micelles were formed around 450 MPa with no variations at higher pr...

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Autores: Bravo, Francisca I., Felipe, Xavier, López-Fandiño, Rosina, Molina, Elena
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2015
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/149976
Acceso en línea:http://hdl.handle.net/10261/149976
Access Level:acceso abierto
Palabra clave:Whey proteins
Very high hydrostatic pressure
Casein
Milk protein distribution
Lactoferrin
Secretory IgA
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spelling Skim milk protein distribution as a result of very high hydrostatic pressureBravo, Francisca I.Felipe, XavierLópez-Fandiño, RosinaMolina, ElenaWhey proteinsVery high hydrostatic pressureCaseinMilk protein distributionLactoferrinSecretory IgAThis work studies the micellar size and the distribution of caseins, major and minor whey proteins in different fractions of skim milk treated up to 900 MPa for 5 min. Transmission electron microscopy showed that the smallest casein micelles were formed around 450 MPa with no variations at higher pressures. The changes found in micellar size correlated with the concentration of soluble casein, because treatments at 250 MPa significantly enhanced the level of non-sedimentable casein while, between 700 and 900 MPa, there were no further increases with respect to lower pressures. There was a severe β-lactoglobulin (β-Lg) denaturation at pressures ≥ 700 MPa, which reached 77–87%. α-Lactalbumin (α-La) was stable up to 550 MPa, but it denatured at higher pressures. The content of soluble lactoferrin (Lf) decreased with pressure, particularly from 550 to 800 MPa, while that of secretory IgA (sIgA) progressively decreased from 250 up to 700 MPa. Our results indicated that treatment of milk at very high pressures, from 700 to 900 MPa, did not reduce micellar size nor released more soluble casein with respect to treatments at lower pressures (250–550 MPa). However, these treatments led to a severe denaturation of the whey proteins, in particular of β-Lg and the minor proteins Lf and sIgA. The possibility of using high hydrostatic pressure to obtain a soluble milk fraction with a casein and whey protein composition similar to that of human milk is discussed.This work received financial support from the project CENIT-2007-2016Futural, Ingenio Program.Peer reviewedPeer ReviewedElsevierConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2017201720152017info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Postprintinfo:eu-repo/semantics/acceptedVersionapplication/pdfhttp://hdl.handle.net/10261/149976reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)InglésSíinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/1499762026-05-22T06:33:51Z
dc.title.none.fl_str_mv Skim milk protein distribution as a result of very high hydrostatic pressure
title Skim milk protein distribution as a result of very high hydrostatic pressure
spellingShingle Skim milk protein distribution as a result of very high hydrostatic pressure
Bravo, Francisca I.
Whey proteins
Very high hydrostatic pressure
Casein
Milk protein distribution
Lactoferrin
Secretory IgA
title_short Skim milk protein distribution as a result of very high hydrostatic pressure
title_full Skim milk protein distribution as a result of very high hydrostatic pressure
title_fullStr Skim milk protein distribution as a result of very high hydrostatic pressure
title_full_unstemmed Skim milk protein distribution as a result of very high hydrostatic pressure
title_sort Skim milk protein distribution as a result of very high hydrostatic pressure
dc.creator.none.fl_str_mv Bravo, Francisca I.
Felipe, Xavier
López-Fandiño, Rosina
Molina, Elena
author Bravo, Francisca I.
author_facet Bravo, Francisca I.
Felipe, Xavier
López-Fandiño, Rosina
Molina, Elena
author_role author
author2 Felipe, Xavier
López-Fandiño, Rosina
Molina, Elena
author2_role author
author
author
dc.contributor.none.fl_str_mv Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Whey proteins
Very high hydrostatic pressure
Casein
Milk protein distribution
Lactoferrin
Secretory IgA
topic Whey proteins
Very high hydrostatic pressure
Casein
Milk protein distribution
Lactoferrin
Secretory IgA
description This work studies the micellar size and the distribution of caseins, major and minor whey proteins in different fractions of skim milk treated up to 900 MPa for 5 min. Transmission electron microscopy showed that the smallest casein micelles were formed around 450 MPa with no variations at higher pressures. The changes found in micellar size correlated with the concentration of soluble casein, because treatments at 250 MPa significantly enhanced the level of non-sedimentable casein while, between 700 and 900 MPa, there were no further increases with respect to lower pressures. There was a severe β-lactoglobulin (β-Lg) denaturation at pressures ≥ 700 MPa, which reached 77–87%. α-Lactalbumin (α-La) was stable up to 550 MPa, but it denatured at higher pressures. The content of soluble lactoferrin (Lf) decreased with pressure, particularly from 550 to 800 MPa, while that of secretory IgA (sIgA) progressively decreased from 250 up to 700 MPa. Our results indicated that treatment of milk at very high pressures, from 700 to 900 MPa, did not reduce micellar size nor released more soluble casein with respect to treatments at lower pressures (250–550 MPa). However, these treatments led to a severe denaturation of the whey proteins, in particular of β-Lg and the minor proteins Lf and sIgA. The possibility of using high hydrostatic pressure to obtain a soluble milk fraction with a casein and whey protein composition similar to that of human milk is discussed.
publishDate 2015
dc.date.none.fl_str_mv 2015
2017
2017
2017
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Postprint
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/149976
url http://hdl.handle.net/10261/149976
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv
dc.rights.none.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 Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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