Structural, Binding and Functional Properties of Milk Protein-Polyphenol Systems: A Review

Polyphenols (PP) are linked to health benefits (e.g., prevention of cancer, cardiovascular disease and obesity), which are mainly attributed to their antioxidant activity. During digestion, PP are oxidised to a significant degree reducing their bio-functionality. In recent years, the potential of va...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Molecules (Basel, Switzerland) Jg. 28; H. 5; S. 2288
Hauptverfasser:	van de Langerijt, Tessa M., O’Mahony, James A., Crowley, Shane V.
Format:	Journal Article
Sprache:	Englisch
Veröffentlicht:	Switzerland MDPI AG 01.03.2023 MDPI
Schlagworte:	aggregates Amino acids Antioxidants Bioavailability blood serum albumin aggregates Calcium phosphates Caseins - chemistry Chemical bonds Chemical properties Chemical research Chemical structure Hydrogen bonds Lactoglobulins Micelles Milk Milk proteins Milk Proteins - chemistry native casein micelles Nutrition research Physicochemical properties Polyphenols Proteins Review Ireland polyphenols blood serum albumin aggregates re-assembled casein micelles aggregates complex formation micelles protein-polyphenol interaction milk proteins native casein micelles casein nanoparticles
ISSN:	1420-3049, 1420-3049
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Abstract	Polyphenols (PP) are linked to health benefits (e.g., prevention of cancer, cardiovascular disease and obesity), which are mainly attributed to their antioxidant activity. During digestion, PP are oxidised to a significant degree reducing their bio-functionality. In recent years, the potential of various milk protein systems, including β-casein micelles, β-lactoglobulin aggregates, blood serum albumin aggregates, native casein micelles and re-assembled casein micelles, to bind and protect PP have been investigated. These studies have yet to be systematically reviewed. The functional properties of the milk protein-PP systems depend on the type and concentration of both PP and protein, as well as the structure of the resultant complexes, with environmental and processing factors also having an influence. Milk protein systems protect PP from degradation during digestion, resulting in a higher bioaccessibility and bioavailability, which improve the functional properties of PP upon consumption. This review compares different milk protein systems in terms of physicochemical properties, PP binding performance and ability to enhance the bio-functional properties of PP. The goal is to provide a comprehensive overview on the structural, binding, and functional properties of milk protein-polyphenol systems. It is concluded that milk protein complexes function effectively as delivery systems for PP, protecting PP from oxidation during digestion.
AbstractList	Polyphenols (PP) are linked to health benefits (e.g., prevention of cancer, cardiovascular disease and obesity), which are mainly attributed to their antioxidant activity. During digestion, PP are oxidised to a significant degree reducing their bio-functionality. In recent years, the potential of various milk protein systems, including β-casein micelles, β-lactoglobulin aggregates, blood serum albumin aggregates, native casein micelles and re-assembled casein micelles, to bind and protect PP have been investigated. These studies have yet to be systematically reviewed. The functional properties of the milk protein-PP systems depend on the type and concentration of both PP and protein, as well as the structure of the resultant complexes, with environmental and processing factors also having an influence. Milk protein systems protect PP from degradation during digestion, resulting in a higher bioaccessibility and bioavailability, which improve the functional properties of PP upon consumption. This review compares different milk protein systems in terms of physicochemical properties, PP binding performance and ability to enhance the bio-functional properties of PP. The goal is to provide a comprehensive overview on the structural, binding, and functional properties of milk protein-polyphenol systems. It is concluded that milk protein complexes function effectively as delivery systems for PP, protecting PP from oxidation during digestion. Polyphenols (PP) are linked to health benefits (e.g., prevention of cancer, cardiovascular disease and obesity), which are mainly attributed to their antioxidant activity. During digestion, PP are oxidised to a significant degree reducing their bio-functionality. In recent years, the potential of various milk protein systems, including β-casein micelles, β-lactoglobulin aggregates, blood serum albumin aggregates, native casein micelles and re-assembled casein micelles, to bind and protect PP have been investigated. These studies have yet to be systematically reviewed. The functional properties of the milk protein-PP systems depend on the type and concentration of both PP and protein, as well as the structure of the resultant complexes, with environmental and processing factors also having an influence. Milk protein systems protect PP from degradation during digestion, resulting in a higher bioaccessibility and bioavailability, which improve the functional properties of PP upon consumption. This review compares different milk protein systems in terms of physicochemical properties, PP binding performance and ability to enhance the bio-functional properties of PP. The goal is to provide a comprehensive overview on the structural, binding, and functional properties of milk protein-polyphenol systems. It is concluded that milk protein complexes function effectively as delivery systems for PP, protecting PP from oxidation during digestion.Polyphenols (PP) are linked to health benefits (e.g., prevention of cancer, cardiovascular disease and obesity), which are mainly attributed to their antioxidant activity. During digestion, PP are oxidised to a significant degree reducing their bio-functionality. In recent years, the potential of various milk protein systems, including β-casein micelles, β-lactoglobulin aggregates, blood serum albumin aggregates, native casein micelles and re-assembled casein micelles, to bind and protect PP have been investigated. These studies have yet to be systematically reviewed. The functional properties of the milk protein-PP systems depend on the type and concentration of both PP and protein, as well as the structure of the resultant complexes, with environmental and processing factors also having an influence. Milk protein systems protect PP from degradation during digestion, resulting in a higher bioaccessibility and bioavailability, which improve the functional properties of PP upon consumption. This review compares different milk protein systems in terms of physicochemical properties, PP binding performance and ability to enhance the bio-functional properties of PP. The goal is to provide a comprehensive overview on the structural, binding, and functional properties of milk protein-polyphenol systems. It is concluded that milk protein complexes function effectively as delivery systems for PP, protecting PP from oxidation during digestion.
Audience	Academic
Author	van de Langerijt, Tessa M. Crowley, Shane V. O’Mahony, James A.
AuthorAffiliation	School of Food and Nutritional Sciences, University College Cork, T12 YN60 Cork, Ireland
AuthorAffiliation_xml	– name: School of Food and Nutritional Sciences, University College Cork, T12 YN60 Cork, Ireland
Author_xml	– sequence: 1 givenname: Tessa M. orcidid: 0000-0001-5852-9650 surname: van de Langerijt fullname: van de Langerijt, Tessa M. – sequence: 2 givenname: James A. orcidid: 0000-0002-1232-741X surname: O’Mahony fullname: O’Mahony, James A. – sequence: 3 givenname: Shane V. surname: Crowley fullname: Crowley, Shane V.
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/36903537$$D View this record in MEDLINE/PubMed
BookMark	eNp9Uk1v1DAUjFARbRd-ABcUiQsHtvgzsbmgpaJQqYiKwoWL5TjPWy-OvdhJ0f57vN1StUVCPth6nhnPe57Dai_EAFX1HKMjSiV6M0QPZvKQiUCcECEeVQeYETSniMm9O-f96jDnFUIEM8yfVPu0kYhy2h5UPy7GNJlxStq_rt-70LuwrHXo65MpmNHFoH19nuIa0ugg19HWn53_uS2N4ML8PPrN-hJC9PXFJo8w5Lf1ov4KVw5-P60eW-0zPLvZZ9X3kw_fjj_Nz758PD1enM0Np3Sca5BtI9qet6UHLEESarAVXdNT3knTU0s409J2vGmYJdJIzWnXNo2x0lJE6Kw63en2Ua_UOrlBp42K2qnrQkxLpYt740GhDgsQumVthxnvuKCoQR2HpkfEasyK1rud1nrqBugNhLFM5p7o_ZvgLtUyXimMEOKMiaLw6kYhxV8T5FENLhvwXgeIU1akFQ2SpPgv0JcPoKs4pTLxa1QZBmXlm2bV0Q611KUDF2wsD5uyehicKYGwrtQXLcOCccRwIby428Ot-b-fXgB4BzAp5pzA3kIwUttgqX-CVTjtA45xo94GpLhx_j_MPym31Hg
CitedBy_id	crossref_primary_10_1002_fsn3_3917 crossref_primary_10_1111_1541_4337_70053 crossref_primary_10_3390_pr11051459 crossref_primary_10_1111_1471_0307_12987 crossref_primary_10_12944_CRNFSJ_13_Special_Issue_July_01 crossref_primary_10_1016_j_idairyj_2025_106420 crossref_primary_10_3390_polym16131818 crossref_primary_10_1016_j_foodhyd_2024_110040 crossref_primary_10_3390_molecules28248081 crossref_primary_10_1016_j_fbio_2025_106278 crossref_primary_10_3390_ijms26188813 crossref_primary_10_1002_jsfa_70010 crossref_primary_10_1016_j_cis_2025_103424 crossref_primary_10_3390_fermentation11050291 crossref_primary_10_1016_j_foodres_2025_116454 crossref_primary_10_1016_j_fbio_2023_103509 crossref_primary_10_1111_ijfs_16722 crossref_primary_10_3390_antiox14010055 crossref_primary_10_3390_micro5030036 crossref_primary_10_1016_j_foodres_2025_116771 crossref_primary_10_1016_j_lwt_2024_117065
Cites_doi	10.1016/j.ijpharm.2019.118652 10.1016/S0958-6946(98)00040-5 10.1016/S0021-9797(02)00066-8 10.3168/jds.2007-0819 10.1016/j.foodres.2014.12.005 10.1016/j.tifs.2010.08.003 10.1016/j.jff.2018.10.025 10.1080/1040869059096 10.1016/j.foodchem.2011.01.079 10.1016/j.jconrel.2011.02.010 10.1016/j.foodhyd.2015.11.007 10.1039/C4SM00239C 10.1111/j.1750-3841.2007.00274.x 10.1016/j.cofs.2016.02.002 10.1016/j.foodchem.2012.11.016 10.1016/j.cofs.2019.10.009 10.1016/j.ijbiomac.2019.04.166 10.3168/jds.S0022-0302(92)77964-8 10.1021/la0632575 10.1016/j.fbp.2019.03.003 10.1051/lait:2002017 10.1111/j.1365-2621.2009.02077.x 10.1016/j.foodhyd.2010.11.025 10.1016/S0065-3233(08)60554-9 10.1039/C7FO01923H 10.3168/jds.2020-18605 10.1016/j.foodres.2013.02.009 10.1016/j.foodchem.2017.07.126 10.1529/biophysj.106.094342 10.1007/s13228-014-0035-y 10.1016/j.foodhyd.2013.07.008 10.1016/j.jamcollsurg.2006.01.018 10.1073/pnas.94.26.14930 10.1016/j.foodhyd.2015.04.036 10.1111/1750-3841.14293 10.1007/978-1-4419-8602-3 10.1016/j.jfoodeng.2015.05.032 10.1111/j.1432-1033.1988.tb14103.x 10.1186/1477-3155-9-19 10.1016/j.jff.2017.10.038 10.1016/j.foodhyd.2015.04.015 10.1016/j.saa.2011.07.028 10.3389/fnut.2021.689456 10.1152/ajpendo.00106.2012 10.1016/j.foodhyd.2012.01.016 10.1021/jf200718j 10.1016/j.foodchem.2020.127209 10.1016/S0927-7757(02)00371-0 10.1016/j.foodhyd.2018.08.031 10.1016/0167-4889(88)90093-6 10.1016/j.foodchem.2013.08.076 10.1016/j.jff.2019.05.053 10.1039/C5FO00829H 10.1039/C5FO01499A 10.1016/j.foodhyd.2019.06.005 10.1016/j.foodchem.2013.03.037 10.1016/j.foodhyd.2014.02.006 10.1002/fsn3.827 10.1016/j.lwt.2011.05.023 10.1111/j.1365-2621.1991.tb08638.x 10.1093/jn/134.12.3431S 10.3109/09637486.2013.849662 10.1016/j.foodhyd.2007.09.002 10.3168/jds.2017-12623 10.1016/j.foodhyd.2018.11.008 10.1016/j.foodhyd.2011.02.006 10.1016/j.jff.2012.05.008 10.1016/j.nano.2010.01.003 10.1080/10942912.2013.853185 10.1016/j.foodhyd.2017.10.008 10.1016/j.foodhyd.2010.03.015 10.1002/mnfr.200500109 10.1007/978-1-4614-4714-6 10.1016/B978-0-12-812124-5.00001-1 10.1016/j.foodhyd.2006.09.006 10.1016/j.foodchem.2013.07.092 10.1016/j.foodhyd.2020.105989 10.1016/j.foodchem.2009.12.064 10.1039/C0SM00806K 10.1039/D0FO00186D 10.1016/j.foodchem.2011.11.019 10.1080/10408399309527643 10.1021/bm800683f 10.1016/j.foodhyd.2014.03.022 10.1021/jf400752a
ContentType	Journal Article
Copyright	COPYRIGHT 2023 MDPI AG 2023 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. 2023 by the authors. 2023
Copyright_xml	– notice: COPYRIGHT 2023 MDPI AG – notice: 2023 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. – notice: 2023 by the authors. 2023
DBID	AAYXX CITATION CGR CUY CVF ECM EIF NPM 3V. 7X7 7XB 88E 8FI 8FJ 8FK ABUWG AFKRA AZQEC BENPR CCPQU DWQXO FYUFA GHDGH K9. M0S M1P PHGZM PHGZT PIMPY PJZUB PKEHL PPXIY PQEST PQQKQ PQUKI PRINS 7X8 5PM DOA
DOI	10.3390/molecules28052288
DatabaseName	CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed ProQuest Central (Corporate) Health & Medical Collection ProQuest Central (purchase pre-March 2016) Medical Database (Alumni Edition) Hospital Premium Collection Hospital Premium Collection (Alumni Edition) ProQuest Central (Alumni) (purchase pre-March 2016) ProQuest Central (Alumni) ProQuest Central UK/Ireland ProQuest Central Essentials ProQuest Central ProQuest One ProQuest Central Health Research Premium Collection Health Research Premium Collection (Alumni) ProQuest Health & Medical Complete (Alumni) ProQuest Health & Medical Collection Medical Database ProQuest Central Premium ProQuest One Academic Publicly Available Content Database ProQuest Health & Medical Research Collection ProQuest One Academic Middle East (New) ProQuest One Health & Nursing ProQuest One Academic Eastern Edition (DO NOT USE) ProQuest One Academic (retired) ProQuest One Academic UKI Edition ProQuest Central China MEDLINE - Academic PubMed Central (Full Participant titles) DOAJ Directory of Open Access Journals
DatabaseTitle	CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) Publicly Available Content Database ProQuest One Academic Middle East (New) ProQuest Central Essentials ProQuest Health & Medical Complete (Alumni) ProQuest Central (Alumni Edition) ProQuest One Community College ProQuest One Health & Nursing ProQuest Central China ProQuest Central ProQuest Health & Medical Research Collection Health Research Premium Collection Health and Medicine Complete (Alumni Edition) ProQuest Central Korea Health & Medical Research Collection ProQuest Central (New) ProQuest Medical Library (Alumni) ProQuest One Academic Eastern Edition ProQuest Hospital Collection Health Research Premium Collection (Alumni) ProQuest Hospital Collection (Alumni) ProQuest Health & Medical Complete ProQuest Medical Library ProQuest One Academic UKI Edition ProQuest One Academic ProQuest One Academic (New) ProQuest Central (Alumni) MEDLINE - Academic
DatabaseTitleList	MEDLINE - Academic Publicly Available Content Database CrossRef MEDLINE
Database_xml	– sequence: 1 dbid: DOA name: DOAJ (Directory of Open Access Journals) url: https://www.doaj.org/ sourceTypes: Open Website – sequence: 2 dbid: NPM name: PubMed url: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 3 dbid: PIMPY name: Publicly Available Content Database url: http://search.proquest.com/publiccontent sourceTypes: Aggregation Database
DeliveryMethod	fulltext_linktorsrc
Discipline	Chemistry
EISSN	1420-3049
ExternalDocumentID	oai_doaj_org_article_0b18e8a747b145b583060b5e6d02fa14 PMC10005448 A741845041 36903537 10_3390_molecules28052288
Genre	Journal Article Review
GeographicLocations	Ireland
GeographicLocations_xml	– name: Ireland
GrantInformation_xml	– fundername: Department of Agriculture, Food and the Marine, Ireland grantid: 17F277 – fundername: Department of Agriculture, Food and the Marine of the Irish Government, under the Food Institutional Research Measure (FIRM) grantid: 17F277
GroupedDBID	--- 0R~ 123 2WC 53G 5VS 7X7 88E 8FE 8FG 8FH 8FI 8FJ A8Z AADQD AAFWJ AAHBH AAYXX ABDBF ABUWG ACGFO ACIWK ACPRK ACUHS AEGXH AENEX AFFHD AFKRA AFPKN AFRAH AFZYC AIAGR ALMA_UNASSIGNED_HOLDINGS BENPR BPHCQ BVXVI CCPQU CITATION CS3 D1I DIK DU5 E3Z EBD EMOBN ESTFP ESX FYUFA GROUPED_DOAJ GX1 HH5 HMCUK HYE HZ~ I09 IAO IHR ITC KQ8 LK8 M1P MODMG O-U O9- OK1 P2P PHGZM PHGZT PIMPY PJZUB PPXIY PQQKQ PROAC PSQYO RPM SV3 TR2 TUS UKHRP ~8M ALIPV CGR CUY CVF ECM EIF NPM 3V. 7XB 8FK AZQEC DWQXO K9. PKEHL PQEST PQUKI PRINS 7X8 PUEGO 5PM
ID	FETCH-LOGICAL-c533t-ae97687d5705219e923c1f8b6d35b9cd3f254a9fb5664f29c9a53b766cf9f3023
IEDL.DBID	7X7
ISICitedReferencesCount	25
ISICitedReferencesURI	http://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestLinkType=CitingArticles&DestApp=WOS_CPL&KeyUT=000947601700001&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D
ISSN	1420-3049
IngestDate	Mon Nov 10 04:31:44 EST 2025 Tue Nov 04 02:07:36 EST 2025 Thu Oct 02 09:57:32 EDT 2025 Sat Nov 29 14:59:35 EST 2025 Tue Nov 04 18:28:25 EST 2025 Mon Jul 21 06:00:48 EDT 2025 Sat Nov 29 07:17:44 EST 2025 Tue Nov 18 21:56:32 EST 2025
IsDoiOpenAccess	true
IsOpenAccess	true
IsPeerReviewed	true
IsScholarly	true
Issue	5
Keywords	polyphenols blood serum albumin aggregates re-assembled casein micelles aggregates complex formation micelles protein-polyphenol interaction milk proteins native casein micelles casein nanoparticles
Language	English
License	Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
LinkModel	DirectLink
MergedId	FETCHMERGED-LOGICAL-c533t-ae97687d5705219e923c1f8b6d35b9cd3f254a9fb5664f29c9a53b766cf9f3023
Notes	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 ObjectType-Review-3 content type line 23
ORCID	0000-0001-5852-9650 0000-0002-1232-741X
OpenAccessLink	https://www.proquest.com/docview/2785213490?pq-origsite=%requestingapplication%
PMID	36903537
PQID	2785213490
PQPubID	2032355
ParticipantIDs	doaj_primary_oai_doaj_org_article_0b18e8a747b145b583060b5e6d02fa14 pubmedcentral_primary_oai_pubmedcentral_nih_gov_10005448 proquest_miscellaneous_2786092766 proquest_journals_2785213490 gale_infotracacademiconefile_A741845041 pubmed_primary_36903537 crossref_primary_10_3390_molecules28052288 crossref_citationtrail_10_3390_molecules28052288
PublicationCentury	2000
PublicationDate	2023-03-01
PublicationDateYYYYMMDD	2023-03-01
PublicationDate_xml	– month: 03 year: 2023 text: 2023-03-01 day: 01
PublicationDecade	2020
PublicationPlace	Switzerland
PublicationPlace_xml	– name: Switzerland – name: Basel
PublicationTitle	Molecules (Basel, Switzerland)
PublicationTitleAlternate	Molecules
PublicationYear	2023
Publisher	MDPI AG MDPI
Publisher_xml	– name: MDPI AG – name: MDPI
References	Boirie (ref_31) 1997; 94 ref_93 Haratifar (ref_44) 2014; 143 Esparza (ref_52) 2019; 570 ref_91 Barraquio (ref_62) 1991; 56 Holt (ref_18) 1992; Volume 43 Esmaili (ref_11) 2011; 44 ref_14 Guyonnet (ref_6) 2021; 8 (ref_65) 2013; 138 Sumpio (ref_94) 2006; 202 Loewen (ref_70) 2018; 240 Moeiniafshari (ref_26) 2015; 51 Pan (ref_51) 2014; 10 Rocchi (ref_55) 2015; 167 Zagury (ref_86) 2019; 52 Malekhosseini (ref_48) 2019; 7 ref_17 Hudson (ref_42) 2019; 133 ref_16 Morr (ref_92) 1993; 33 ref_15 Bah (ref_49) 2018; 83 Schuck (ref_61) 2002; 82 Okun (ref_3) 2020; 31 Crespy (ref_96) 2004; 134 Zhang (ref_9) 2016; 8 Chanphai (ref_24) 2018; 77 Pilosof (ref_82) 2015; 50 Fang (ref_36) 2011; 59 Griffin (ref_57) 1988; 174 Crowley (ref_47) 2021; 154 Fang (ref_35) 2011; 9 ref_25 Oliveira (ref_79) 2016; 55 Shpigelman (ref_84) 2010; 24 Acharya (ref_59) 2013; 141 (ref_2) 2009; 44 ref_22 Chanphai (ref_89) 2019; 89 Elzoghby (ref_30) 2011; 153 ref_63 Jara (ref_81) 2012; 4 Li (ref_53) 2019; 96 Cheng (ref_56) 2020; 330 Shapira (ref_73) 2010; 6 HadjSadok (ref_64) 2008; 22 Parada (ref_8) 2007; 72 Sousa (ref_28) 2014; 65 Scalbert (ref_5) 2005; 45 Khanji (ref_41) 2015; 6 Grinberg (ref_74) 2002; 210 Schneider (ref_33) 2016; 7 ref_72 Yazdi (ref_38) 2014; 42 Nadi (ref_40) 2015; 18 Khanji (ref_43) 2018; 9 Zimet (ref_66) 2011; 25 Pilosof (ref_80) 2014; 35 Fang (ref_7) 2010; 21 Ghatak (ref_50) 2019; 115 Horne (ref_19) 1998; 8 Yazdi (ref_21) 2012; 132 Zhang (ref_37) 2014; 145 ref_75 Thongkaew (ref_78) 2014; 41 Grinberg (ref_60) 2003; 258 Hindmarsh (ref_67) 2017; 100 Guri (ref_46) 2014; 5 Yuksel (ref_45) 2010; 121 Zagury (ref_87) 2019; 59 Kanakis (ref_83) 2011; 127 Diaz (ref_34) 2020; 11 Wu (ref_88) 2017; 39 Semo (ref_58) 2007; 21 Schmitt (ref_76) 2007; 23 Shpigelman (ref_85) 2012; 29 Kao (ref_95) 2006; 50 McClements (ref_77) 2015; 69 Dumpler (ref_29) 2020; 103 Li (ref_54) 2020; 108 Sahu (ref_39) 2008; 9 ref_1 Ghayour (ref_12) 2019; 87 Nicolai (ref_23) 2011; 25 DePeters (ref_13) 1992; 75 McMahon (ref_69) 2008; 91 Krebs (ref_90) 2007; 92 Wu (ref_27) 2011; 82 Dalgleish (ref_20) 2011; 7 Ozdal (ref_68) 2013; 51 Pfaff (ref_71) 1988; 969 Pan (ref_10) 2013; 61 Soop (ref_32) 2012; 303 ref_4
References_xml	– volume: 570 start-page: 118652 year: 2019 ident: ref_52 article-title: Casein nanoparticles in combination with 2-hydroxypropyl-β-cyclodextrin improves the oral bioavailability of quercetin publication-title: Int. J. Pharm. doi: 10.1016/j.ijpharm.2019.118652 – volume: 8 start-page: 171 year: 1998 ident: ref_19 article-title: Casein interactions: Casting light on the black boxes, the structure in dairy products publication-title: Int. Dairy J. doi: 10.1016/S0958-6946(98)00040-5 – volume: 258 start-page: 33 year: 2003 ident: ref_60 article-title: Association behavior of β-casein publication-title: J. Colloid Interface Sci. doi: 10.1016/S0021-9797(02)00066-8 – volume: 91 start-page: 1709 year: 2008 ident: ref_69 article-title: Supramolecular structure of the casein micelle publication-title: J. Dairy Sci. doi: 10.3168/jds.2007-0819 – volume: 69 start-page: 1 year: 2015 ident: ref_77 article-title: Biopolymer nanoparticles as potential delivery systems for anthocyanins: Fabrication and properties publication-title: Food Res. Int. doi: 10.1016/j.foodres.2014.12.005 – volume: 21 start-page: 510 year: 2010 ident: ref_7 article-title: Encapsulation of polyphenols-A review publication-title: Trends Food Sci. Technol. doi: 10.1016/j.tifs.2010.08.003 – volume: 52 start-page: 121 year: 2019 ident: ref_86 article-title: Improved antioxidant activity, bioaccessibility and bioavailability of EGCG by delivery in β-lactoglobulin particles publication-title: J. Funct. Foods doi: 10.1016/j.jff.2018.10.025 – volume: 45 start-page: 287 year: 2005 ident: ref_5 article-title: Dietary polyphenols and the prevention of diseases publication-title: Crit. Rev. Food Sci. Nutr. doi: 10.1080/1040869059096 – volume: 127 start-page: 1046 year: 2011 ident: ref_83 article-title: Milk β-lactoglobulin complexes with tea polyphenols publication-title: Food Chem. doi: 10.1016/j.foodchem.2011.01.079 – volume: 153 start-page: 206 year: 2011 ident: ref_30 article-title: Casein-based formulations as promising controlled release drug delivery systems publication-title: J. Control. Release doi: 10.1016/j.jconrel.2011.02.010 – volume: 55 start-page: 119 year: 2016 ident: ref_79 article-title: Impact of pectin or chitosan on bulk, interfacial and antioxidant properties of (+)-catechin and β-lactoglobulin ternary mixtures publication-title: Food Hydrocoll. doi: 10.1016/j.foodhyd.2015.11.007 – volume: 10 start-page: 6820 year: 2014 ident: ref_51 article-title: PH-driven encapsulation of curcumin in self-assembled casein nanoparticles for enhanced dispersibility and bioactivity publication-title: Soft Matter doi: 10.1039/C4SM00239C – volume: 72 start-page: 21 year: 2007 ident: ref_8 article-title: Food microstructure affects the bioavailability of several nutrients publication-title: J. Food Sci. doi: 10.1111/j.1750-3841.2007.00274.x – volume: 8 start-page: 33 year: 2016 ident: ref_9 article-title: Dietary polyphenols, oxidative stress and antioxidant and anti-inflammatory effects publication-title: Curr. Opin. Food Sci. doi: 10.1016/j.cofs.2016.02.002 – volume: 138 start-page: 1581 year: 2013 ident: ref_65 article-title: Thermal protection of β-carotene in re-assembled casein micelles during different processing technologies applied in food industry publication-title: Food Chem. doi: 10.1016/j.foodchem.2012.11.016 – volume: 31 start-page: 38 year: 2020 ident: ref_3 article-title: Digestive fate of polyphenols: Updated view of the influence of chemical structure and the presence of cell wall material publication-title: Curr. Opin. Food Sci. doi: 10.1016/j.cofs.2019.10.009 – volume: 133 start-page: 860 year: 2019 ident: ref_42 article-title: Curcumin-micellar casein multisite interactions elucidated by surface plasmon resonance publication-title: Int. J. Biol. Macromol. doi: 10.1016/j.ijbiomac.2019.04.166 – ident: ref_1 – volume: 75 start-page: 2043 year: 1992 ident: ref_13 article-title: Nutritional Factors Influencing the Nitrogen Composition of Bovine Milk: A Review publication-title: J. Dairy Sci. doi: 10.3168/jds.S0022-0302(92)77964-8 – volume: 23 start-page: 4155 year: 2007 ident: ref_76 article-title: Whey protein soluble aggregates from heating with NaCl: Physicochemical, interfacial, and foaming properties publication-title: Langmuir doi: 10.1021/la0632575 – volume: 115 start-page: 100 year: 2019 ident: ref_50 article-title: Selective encapsulation of quercetin from dry onion peel crude extract in reassembled casein particles publication-title: Food Bioprod. Process. doi: 10.1016/j.fbp.2019.03.003 – volume: 82 start-page: 375 year: 2002 ident: ref_61 article-title: Spray Drying of Dairy Products: State of the Art publication-title: Lait doi: 10.1051/lait:2002017 – volume: 44 start-page: 2512 year: 2009 ident: ref_2 article-title: Polyphenols: Food sources, properties and applications-A review publication-title: Int. J. Food Sci. Technol. doi: 10.1111/j.1365-2621.2009.02077.x – volume: 25 start-page: 1270 year: 2011 ident: ref_66 article-title: Re-assembled casein micelles and casein nanoparticles as nano-vehicles for ω-3 polyunsaturated fatty acids publication-title: Food Hydrocoll. doi: 10.1016/j.foodhyd.2010.11.025 – volume: Volume 43 start-page: 63 year: 1992 ident: ref_18 article-title: Structure and Stability of Bovine Casein Micelles publication-title: Advances in Protein Chemistry doi: 10.1016/S0065-3233(08)60554-9 – volume: 9 start-page: 971 year: 2018 ident: ref_43 article-title: Structure, gelation, and antioxidant properties of curcumin-doped casein micelle powder produced by spray-drying publication-title: Food Funct. doi: 10.1039/C7FO01923H – volume: 154 start-page: 112775 year: 2021 ident: ref_47 article-title: The influence of sodium caseinate and β-casein concentrate on the physicochemical properties of casein micelles and the role of tea polyphenols in mediating these interactions publication-title: LWT-Food Sci. Technol. – ident: ref_4 – volume: 103 start-page: 10986 year: 2020 ident: ref_29 article-title: Invited Review: Heat Stability of Milk and Concentrated Milk: Past, Present, and Future Research Objectives publication-title: J. Dairy Sci. doi: 10.3168/jds.2020-18605 – volume: 51 start-page: 954 year: 2013 ident: ref_68 article-title: A review on protein-phenolic interactions and associated changes publication-title: Food Res. Int. doi: 10.1016/j.foodres.2013.02.009 – volume: 240 start-page: 472 year: 2018 ident: ref_70 article-title: Optimization of vitamins A and D3 loading in re-assembled casein micelles and effect of loading on stability of vitamin D3 during storage publication-title: Food Chem. doi: 10.1016/j.foodchem.2017.07.126 – volume: 92 start-page: 1336 year: 2007 ident: ref_90 article-title: Protein particulates: Another generic form of protein aggregation? publication-title: Biophys. J. doi: 10.1529/biophysj.106.094342 – volume: 5 start-page: 8 year: 2014 ident: ref_46 article-title: Bioefficacy of tea catechins associated with milk caseins tested using different In Vitro digestion models publication-title: Food Dig. doi: 10.1007/s13228-014-0035-y – volume: 35 start-page: 505 year: 2014 ident: ref_80 article-title: Green tea polyphenols-β-lactoglobulin nanocomplexes: Interfacial behavior, emulsification and oxidation stability of fish oil publication-title: Food Hydrocoll. doi: 10.1016/j.foodhyd.2013.07.008 – volume: 202 start-page: 813 year: 2006 ident: ref_94 article-title: Green Tea, the “Asian Paradox”, and Cardiovascular Disease publication-title: J. Am. Coll. Surg. doi: 10.1016/j.jamcollsurg.2006.01.018 – volume: 94 start-page: 14930 year: 1997 ident: ref_31 article-title: Slow and fast dietary proteins differently modulate postprandial protein accretion publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.94.26.14930 – volume: 51 start-page: 1 year: 2015 ident: ref_26 article-title: Exploring the interaction of naringenin with bovine beta-casein nanoparticles using spectroscopy publication-title: Food Hydrocoll. doi: 10.1016/j.foodhyd.2015.04.036 – volume: 83 start-page: 2295 year: 2018 ident: ref_49 article-title: Study of the Interactions Occurring During the Encapsulation of Sesamol within Casein Micelles Reformed from Sodium Caseinate Solutions publication-title: J. Food Sci. doi: 10.1111/1750-3841.14293 – ident: ref_17 doi: 10.1007/978-1-4419-8602-3 – volume: 167 start-page: 217 year: 2015 ident: ref_55 article-title: Characterization of resveratrol-milk protein interaction publication-title: J. Food Eng. doi: 10.1016/j.jfoodeng.2015.05.032 – ident: ref_72 – volume: 174 start-page: 339 year: 1988 ident: ref_57 article-title: The disaggregation of calcium-depleted casein micelles publication-title: Eur. J. Biochem. doi: 10.1111/j.1432-1033.1988.tb14103.x – ident: ref_93 – volume: 9 start-page: 19 year: 2011 ident: ref_35 article-title: Design and characterization of protein-quercetin bioactive nanoparticles publication-title: J. Nanobiotechnol. doi: 10.1186/1477-3155-9-19 – volume: 39 start-page: 257 year: 2017 ident: ref_88 article-title: Epigallocatechin gallate-β-lactoglobulin nanoparticles improve the antitumor activity of EGCG for inducing cancer cell apoptosis publication-title: J. Funct. Foods doi: 10.1016/j.jff.2017.10.038 – volume: 50 start-page: 108 year: 2015 ident: ref_82 article-title: Green tea polyphenols-whey proteins nanoparticles: Bulk, interfacial and foaming behavior publication-title: Food Hydrocoll. doi: 10.1016/j.foodhyd.2015.04.015 – volume: 82 start-page: 164 year: 2011 ident: ref_27 article-title: Analysis of binding interaction between (-)-epigallocatechin (EGC) and β-lactoglobulin by multi-spectroscopic method publication-title: Spectrochim. Acta A Mol. Biomol. Spectrosc. doi: 10.1016/j.saa.2011.07.028 – volume: 8 start-page: 689456 year: 2021 ident: ref_6 article-title: Polyphenol-Mediated Gut Microbiota Modulation: Toward Prebiotics and Further publication-title: Front. Nutr. doi: 10.3389/fnut.2021.689456 – volume: 303 start-page: 152 year: 2012 ident: ref_32 article-title: Coingestion of whey protein and casein in a mixed meal: Demonstration of a more sustained anabolic effect of casein publication-title: Am. J. Physiol. Endocrinol. Metab. doi: 10.1152/ajpendo.00106.2012 – volume: 29 start-page: 57 year: 2012 ident: ref_85 article-title: Thermally-induced β-lactoglobulin-EGCG nanovehicles: Loading, stability, sensory and digestive-release study publication-title: Food Hydrocoll. doi: 10.1016/j.foodhyd.2012.01.016 – volume: 59 start-page: 6292 year: 2011 ident: ref_36 article-title: Bovine serum albumin nanoparticle promotes the stability of quercetin in simulated intestinal fluid publication-title: J. Agric. Food Chem. doi: 10.1021/jf200718j – volume: 330 start-page: 127209 year: 2020 ident: ref_56 article-title: A comparison of β-casein complexes and micelles as vehicles for trans-/cis-resveratrol publication-title: Food Chem. doi: 10.1016/j.foodchem.2020.127209 – volume: 210 start-page: 183 year: 2002 ident: ref_74 article-title: Micellisation of β-casein publication-title: Colloids Surf. A Physicochem. Eng. Asp. doi: 10.1016/S0927-7757(02)00371-0 – volume: 87 start-page: 394 year: 2019 ident: ref_12 article-title: Nanoencapsulation of quercetin and curcumin in casein-based delivery systems publication-title: Food Hydrocoll. doi: 10.1016/j.foodhyd.2018.08.031 – volume: 969 start-page: 100 year: 1988 ident: ref_71 article-title: Casein kinase II accumulation in the nucleolus and its role in nucleolar phosphorylation publication-title: Biochim. Biophys. Acta (BBA)-Mol. Cell Res. doi: 10.1016/0167-4889(88)90093-6 – volume: 145 start-page: 473 year: 2014 ident: ref_37 article-title: Effect of initial protein concentration and pH on in vitro gastric digestion of heated whey proteins publication-title: Food Chem. doi: 10.1016/j.foodchem.2013.08.076 – volume: 59 start-page: 362 year: 2019 ident: ref_87 article-title: β-Lactoglobulin delivery system for enhancing EGCG biological efficacy in HFD obesity mice model publication-title: J. Funct. Foods doi: 10.1016/j.jff.2019.05.053 – volume: 6 start-page: 3624 year: 2015 ident: ref_41 article-title: Structure and gelation properties of casein micelles doped with curcumin under acidic conditions publication-title: Food Funct. doi: 10.1039/C5FO00829H – volume: 7 start-page: 1306 year: 2016 ident: ref_33 article-title: Formation of whey protein-polyphenol meso-structures as a natural means of creating functional particles publication-title: Food Funct. doi: 10.1039/C5FO01499A – volume: 96 start-page: 653 year: 2019 ident: ref_53 article-title: Bovine beta-casein micelles as delivery systems for hydrophobic flavonoids publication-title: Food Hydrocoll. doi: 10.1016/j.foodhyd.2019.06.005 – volume: 141 start-page: 1050 year: 2013 ident: ref_59 article-title: Binding of resveratrol with sodium caseinate in aqueous solutions publication-title: Food Chem. doi: 10.1016/j.foodchem.2013.03.037 – volume: 41 start-page: 103 year: 2014 ident: ref_78 article-title: Polyphenol interactions with whey protein isolate and whey protein isolate-pectin coacervates publication-title: Food Hydrocoll. doi: 10.1016/j.foodhyd.2014.02.006 – volume: 7 start-page: 519 year: 2019 ident: ref_48 article-title: Development of casein-based nanoencapsulation systems for delivery of epigallocatechin gallate and folic acid publication-title: Food Sci. Nutr. doi: 10.1002/fsn3.827 – volume: 44 start-page: 2166 year: 2011 ident: ref_11 article-title: Beta casein-micelle as a nano vehicle for solubility enhancement of curcumin; food industry application publication-title: LWT-Food Sci. Technol. doi: 10.1016/j.lwt.2011.05.023 – ident: ref_14 – ident: ref_63 – volume: 56 start-page: 1552 year: 1991 ident: ref_62 article-title: Sodium caseinate from skim milk powder by extrusion processing: Physicochemical and functional properties publication-title: J. Food Sci. doi: 10.1111/j.1365-2621.1991.tb08638.x – volume: 134 start-page: 3431S year: 2004 ident: ref_96 article-title: A review of the health effects of green tea catechins in in vivo animal models publication-title: J. Nutr. doi: 10.1093/jn/134.12.3431S – volume: 65 start-page: 151 year: 2014 ident: ref_28 article-title: Dietary Strategies to Recover from Exercise-Induced Muscle Damage publication-title: Int. J. Food Sci. Nutr. doi: 10.3109/09637486.2013.849662 – volume: 22 start-page: 1460 year: 2008 ident: ref_64 article-title: Characterisation of sodium caseinate as a function of ionic strength, pH and temperature using static and dynamic light scattering publication-title: Food Hydrocoll. doi: 10.1016/j.foodhyd.2007.09.002 – volume: 100 start-page: 6938 year: 2017 ident: ref_67 article-title: Experimental evidence for previously unclassified calcium phosphate structures in the casein micelle publication-title: J. Dairy Sci. doi: 10.3168/jds.2017-12623 – volume: 89 start-page: 461 year: 2019 ident: ref_89 article-title: Tea polyphenols bind serum albumins: A potential application for polyphenol delivery publication-title: Food Hydrocoll. doi: 10.1016/j.foodhyd.2018.11.008 – volume: 25 start-page: 1945 year: 2011 ident: ref_23 article-title: β-Lactoglobulin and WPI aggregates: Formation, structure and applications publication-title: Food Hydrocoll. doi: 10.1016/j.foodhyd.2011.02.006 – volume: 4 start-page: 800 year: 2012 ident: ref_81 article-title: Nanocomplex formation between β-lactoglobulin or caseinomacropeptide and green tea polyphenols: Impact on protein gelation and polyphenols antiproliferative activity publication-title: J. Funct. Foods doi: 10.1016/j.jff.2012.05.008 – volume: 6 start-page: 547 year: 2010 ident: ref_73 article-title: β-casein-based nanovehicles for oral delivery of chemotherapeutic drugs: Drug-protein interactions and mitoxantrone loading capacity publication-title: Nanomedicine doi: 10.1016/j.nano.2010.01.003 – volume: 18 start-page: 638 year: 2015 ident: ref_40 article-title: Comparative spectroscopic studies on curcumin stabilization by association to bovine serum albumin and casein: A Perspective on drug-delivery application publication-title: Int. J. Food Prop. doi: 10.1080/10942912.2013.853185 – volume: 77 start-page: 322 year: 2018 ident: ref_24 article-title: Review on the loading efficacy of dietary tea polyphenols with milk proteins publication-title: Food Hydrocoll. doi: 10.1016/j.foodhyd.2017.10.008 – volume: 24 start-page: 735 year: 2010 ident: ref_84 article-title: Thermally-induced protein-polyphenol co-assemblies: Beta lactoglobulin-based nanocomplexes as protective nanovehicles for EGCG publication-title: Food Hydrocoll. doi: 10.1016/j.foodhyd.2010.03.015 – volume: 50 start-page: 188 year: 2006 ident: ref_95 article-title: Tea, obesity, and diabetes publication-title: Mol. Nutr. Food Res. doi: 10.1002/mnfr.200500109 – ident: ref_25 – ident: ref_16 doi: 10.1007/978-1-4614-4714-6 – ident: ref_75 doi: 10.1016/B978-0-12-812124-5.00001-1 – volume: 21 start-page: 936 year: 2007 ident: ref_58 article-title: Casein micelle as a natural nano-capsular vehicle for nutraceuticals publication-title: Food Hydrocoll. doi: 10.1016/j.foodhyd.2006.09.006 – volume: 143 start-page: 27 year: 2014 ident: ref_44 article-title: Interactions between tea catechins and casein micelles and their impact on renneting functionality publication-title: Food Chem. doi: 10.1016/j.foodchem.2013.07.092 – volume: 108 start-page: 105989 year: 2020 ident: ref_54 article-title: Effects of genipin concentration on cross-linked β-casein micelles as nanocarrier of naringenin: Colloidal properties, structural characterization and controlled release publication-title: Food Hydrocoll. doi: 10.1016/j.foodhyd.2020.105989 – ident: ref_15 – ident: ref_91 – volume: 121 start-page: 450 year: 2010 ident: ref_45 article-title: Characterization of binding interactions between green tea flavonoids and milk proteins publication-title: Food Chem. doi: 10.1016/j.foodchem.2009.12.064 – volume: 7 start-page: 2265 year: 2011 ident: ref_20 article-title: On the structural models of bovine casein micelles-Review and possible improvements publication-title: Soft Matter doi: 10.1039/C0SM00806K – ident: ref_22 – volume: 11 start-page: 5091 year: 2020 ident: ref_34 article-title: Formulation of protein-polyphenol particles for applications in food systems publication-title: Food Funct. doi: 10.1039/D0FO00186D – volume: 132 start-page: 1143 year: 2012 ident: ref_21 article-title: Heating of milk alters the binding of curcumin to casein micelles. A fluorescence spectroscopy study publication-title: Food Chem. doi: 10.1016/j.foodchem.2011.11.019 – volume: 33 start-page: 431 year: 1993 ident: ref_92 article-title: Whey Protein Concentrates and Isolates: Processing and Functional Properties publication-title: Crit. Rev. Food Sci. Nutr. doi: 10.1080/10408399309527643 – volume: 9 start-page: 2905 year: 2008 ident: ref_39 article-title: Fluorescence study of the curcumin-casein micelle complexation and its application as a drug nanocarrier to cancer cells publication-title: Biomacromolecules doi: 10.1021/bm800683f – volume: 42 start-page: 171 year: 2014 ident: ref_38 article-title: Studying the structure of β-casein-depleted bovine casein micelles using electron microscopy and fluorescent polyphenols publication-title: Food Hydrocoll. doi: 10.1016/j.foodhyd.2014.03.022 – volume: 61 start-page: 6036 year: 2013 ident: ref_10 article-title: Enhanced dispersibility and bioactivity of curcumin by encapsulation in casein nanocapsules publication-title: J. Agric. Food Chem. doi: 10.1021/jf400752a
SSID	ssj0021415
Score	2.4941106
SecondaryResourceType	review_article
Snippet	Polyphenols (PP) are linked to health benefits (e.g., prevention of cancer, cardiovascular disease and obesity), which are mainly attributed to their...
SourceID	doaj pubmedcentral proquest gale pubmed crossref
SourceType	Open Website Open Access Repository Aggregation Database Index Database Enrichment Source
StartPage	2288
SubjectTerms	aggregates Amino acids Antioxidants Bioavailability blood serum albumin aggregates Calcium phosphates Caseins - chemistry Chemical bonds Chemical properties Chemical research Chemical structure Hydrogen bonds Lactoglobulins Micelles Milk Milk proteins Milk Proteins - chemistry native casein micelles Nutrition research Physicochemical properties Polyphenols Proteins Review
SummonAdditionalLinks	– databaseName: DOAJ Directory of Open Access Journals dbid: DOA link: http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV3fi9QwEB7kEPRF_G31lAiCIJZr0yZNfNs7XHzQY0GFw5eQpAkut7Zyewr-984k3XWXA33xtUlpMjPpzCST7wN44YPsa8ltKbval2gUsbQ2tmXjtQpSRCVDAnF9352eqrMzvdih-qKasAwPnAV3VLlaBWUx6nV1K5xQGONWTuAnKh5torDmVac3ydSUatXol_IZZoNJ_dG3TDUb1pwQ_HmiWfnjhRJY_9Vf8o5P2q-X3HFA89twa4oc2SyP-A5cC8NduHGyIWy7B18-JixYwtF4zY6X6boKs0PP5ui78pYfW9De-wWBqLIxsg_L1Tk9IsbLcjGuflHB17hiE4z5GzZj-ezgPnyev_108q6cqBNKj_HbZWkDhhmq60VHl3N1wDDO11E52TfCad83ERNDq6PDaK6NXHttReM6KX3UkXiEHsDBMA7hEbDoonTBxd7y0IZaOKciClyERre972wB1UaUxk-44kRvsTKYX5D0zRXpF_Bq-8r3DKrxt87HpJ9tR8LDTg_QSsxkJeZfVlLAS9KuoVWLg_N2unyAUyT8KzMjEJ9WVG1dwOHGAMy0nNeGd0oQ9J2uCni-bUb10umKHcL4I_WRleYowwIeZnvZjrmRumpE0xWg9ixpb1L7LcPyawL7rlNU3arH_0MMT-AmR-XmGrpDOECzDE_huv95uVxfPEtL6DdRTyNb priority: 102 providerName: Directory of Open Access Journals
Title	Structural, Binding and Functional Properties of Milk Protein-Polyphenol Systems: A Review
URI	https://www.ncbi.nlm.nih.gov/pubmed/36903537 https://www.proquest.com/docview/2785213490 https://www.proquest.com/docview/2786092766 https://pubmed.ncbi.nlm.nih.gov/PMC10005448 https://doaj.org/article/0b18e8a747b145b583060b5e6d02fa14
Volume	28
WOSCitedRecordID	wos000947601700001&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D
hasFullText	1
inHoldings	1
isFullTextHit
isPrint
journalDatabaseRights	– providerCode: PRVAON databaseName: DOAJ (Directory of Open Access Journals) customDbUrl: eissn: 1420-3049 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0021415 issn: 1420-3049 databaseCode: DOA dateStart: 19970101 isFulltext: true titleUrlDefault: https://www.doaj.org/ providerName: Directory of Open Access Journals – providerCode: PRVPQU databaseName: Health & Medical Collection customDbUrl: eissn: 1420-3049 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0021415 issn: 1420-3049 databaseCode: 7X7 dateStart: 19970101 isFulltext: true titleUrlDefault: https://search.proquest.com/healthcomplete providerName: ProQuest – providerCode: PRVPQU databaseName: ProQuest Central customDbUrl: eissn: 1420-3049 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0021415 issn: 1420-3049 databaseCode: BENPR dateStart: 19970101 isFulltext: true titleUrlDefault: https://www.proquest.com/central providerName: ProQuest – providerCode: PRVPQU databaseName: Publicly Available Content Database customDbUrl: eissn: 1420-3049 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0021415 issn: 1420-3049 databaseCode: PIMPY dateStart: 19970101 isFulltext: true titleUrlDefault: http://search.proquest.com/publiccontent providerName: ProQuest
link	http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1ba9swFD5s7WB72X2dty5oMBiMmVq2JUt9GUlp2GANZhfI9mIkWVrDMrtLusH-fXVkJ2ko9GUvgdgKSDmfdC6Svg_glbG8pjxVMS-oiT0oXKyUy-PMSGE5c4LbQOL6sZhMxHQqy77gtuyPVa7WxLBQ163BGvlBWgiG7GMyeXf2O0bVKNxd7SU0bsIuymYjzovpJuGi3jt1O5mZT-0PfnWCs3aZIo9_GsRWNr4oUPZfXZgveabtU5OX3ND43v8O4D7c7QNQMuwQ8wBu2OYh3D5a6b49gu-fA6Us0nG8JaNZuPVCVFOTsXeBXeWQlFjCXyAXK2kdOZnNf-IjFM6My3b-D8-NtXPSs6EfkiHptiAew9fx8Zej93GvwBAbHwaex8r6aEUUNSvwjq-0Pho01AnN64xpaerM-fxSSad9UJi7VBqpWKYLzo2TDuWInsBO0zb2KRCnHddWu1qlNreUaS1cUkhmM5nXplARJCtbVKanJ0eVjHnl0xQ0X3XFfBG8Wf_krOPmuK7xCA28boi02uFBu_hR9bO0SjQVViifYmmaM82ET6gSzTyek9QpmkfwGuFR4eT3nTOqv8Pgh4g0WtUQuYByluQ0gv0VCqp-VVhWGwhE8HL92psXN2lUY9s_oQ1PZOr_wwj2OsCt-5xxmWQsKyIQW1DcGtT2m2Z2GjjDaQjOc_Hs-n49hzupN1t3yG4fdjzg7Au4Zf6ez5aLQZhd4VMMYHd0PCk_DUIRw38rP5yU3y4ALg03RA
linkProvider	ProQuest
linkToHtml	http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMw1V1baxQxFA6lCvXF-2W0agRFEIfOZCY3QWRbXVq6XRassPgyJpnELl1n6m5V-qf8jeZkZna7FPrWB1-TDCSTL-fk5CTfh9BLY1mZMqJixlMTe1C4WCmXx5mRwjLqBLOBxHXAh0MxHsvRGvrbvYWBa5WdTQyGuqwNnJFvES4osI_J5MPJzxhUoyC72kloNLDYt2d_fMg2f7_30c_vK0L6nw53duNWVSA2fmtzGivrPbDgJeXwblVav8MxqROalRnV0pSZ8zGTkk77jU7uiDRS0UxzxoyTLgtEB97kX_N2nEOwx8fLAC_13rDJnGaZTLZ-NAK3dk5AN4AEcZel7wsSARcdwTlPuHpL85zb69_6337YbXSz3WDjXrMi7qA1W91FGzudrt099PVzoMwFupG3eHsSXvVgVZW47118czKKR5CimAHXLK4dPphMj6EIhEHjUT09g3tx9RS3bO_vcA83KZb76MuVDO0BWq_qyj5C2GnHtNWuVMTmNqVaC5dwSW0m89JwFaGkm_vCtPTroAIyLXwYBnApLsAlQm8Wn5w03COXNd4GQC0aAm14KKhn34vWChWJToUVyoeQOs2ppsIHjImmfr0mxKk0j9BrgGMBxs13zqj2jYYfItCEFT3gOsppkqcR2uxQV7RWb14sIRehF4tqP72QhFKVrX-FNiyRxP_DCD1sAL7oc8ZkktGMR0isQH9lUKs11eQocKKnIfjIxePL-_UcbeweHgyKwd5w_wm6QfwUNhcKN9G6B599iq6b36eT-exZWNkYfbvqlfEPPzqOCQ
linkToPdf	http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMw1V1Lb9QwEB5VLQIuvB-BAkYCISGiJnac2EgIbVtWrNquIgFSyyXYjg0rlqTsFlD_Gr-OcR7brir11gPX2JHs-JtXZvwNwDNj0zJOqQrTLDYhgsKFSrkkZEYKm3InUtuQuO5m47HY35f5Cvzt78L4sspeJzaKuqyN_0e-QTPBPfuYjDZcVxaRbw_fHv4MfQcpn2nt22m0ENmxx38wfJu_GW3jWT-ndPju49b7sOswEBp0c45CZdEai6zkmb_DKi16OyZ2Qqcl41qakjmMn5R0Gp2exFFppOJMZ2lqnHSsIT1A9b-GLnlCV2EtH-3lB4twL0bb2OZRGcNV_2jb3do59V0EaNPq5cQSNg0DzpqFU3ZxuWbzlBEcXv-fP98NuNa53mTQyspNWLHVLbiy1Xe8uw2fPzRkup6I5BXZnDT3fYiqSjJE49_-MyW5T17MPAstqR3Zm0y_-0e-ZWiY19NjXzFXT0nHA_-aDEibfLkDny5ka3dhtaorex-I0y7VVrtSUZvYmGstXJRJbplMSpOpAKIeB4XpiNl9f5BpgQGah05xBjoBvFy8ctiykpw3edODazHRE4o3D-rZ16LTT0WkY2GFQiTrOOGaCwwlI81RkiPqVJwE8MJDs_BqDxdnVHd7A7foCcSKgWdBSniUxAGs9wgsOn04L07gF8DTxTAer09PqcrWv5o5aSQpfsMA7rVgX6yZpTJinGUBiCUxWNrU8kg1-dawpcdNWJKIB-ev6wlcRoEodkfjnYdwleIJtpWG67CK2LOP4JL5fTSZzx53Yk7gy0WLxj8y05hY
openUrl	ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Structural%2C+Binding+and+Functional+Properties+of+Milk+Protein-Polyphenol+Systems%3A+A+Review&rft.jtitle=Molecules+%28Basel%2C+Switzerland%29&rft.au=van+de+Langerijt%2C+Tessa+M.&rft.au=O%E2%80%99Mahony%2C+James+A.&rft.au=Crowley%2C+Shane+V.&rft.date=2023-03-01&rft.pub=MDPI&rft.eissn=1420-3049&rft.volume=28&rft.issue=5&rft_id=info:doi/10.3390%2Fmolecules28052288&rft_id=info%3Apmid%2F36903537&rft.externalDocID=PMC10005448
thumbnail_l	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1420-3049&client=summon
thumbnail_m	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1420-3049&client=summon
thumbnail_s	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1420-3049&client=summon