Assembly of food proteins for nano- encapsulation and delivery of nutraceuticals (a mini-review)

Incorporation of hydrophobic and poorly soluble nutraceuticals into food formulations is among the great challenges in food science and pharmaceutical fields. One effective strategy to meet this challenge is to develop a kind of food-compatible nanovehicles for improving water solubility, stability,...

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Vydané v:Food hydrocolloids Ročník 117; s. 106710
Hlavný autor: Tang, Chuan-He
Médium: Journal Article
Jazyk:English
Vydavateľské údaje: Elsevier Ltd 01.08.2021
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Abstract Incorporation of hydrophobic and poorly soluble nutraceuticals into food formulations is among the great challenges in food science and pharmaceutical fields. One effective strategy to meet this challenge is to develop a kind of food-compatible nanovehicles for improving water solubility, stability, bioavailability and bioactivities of these nutraceuticals. Many food protein-based nano-architectures, e.g., nanoparticles, nano-complexes, nanogels, nano-micelles, nanofibers or nanotubes, have been demonstrated to perform as outstanding nanovehicles in this regard. They are not only nutritional/digestible, safe, and easy to prepare and handle, but also have high encapsulation performance and nutraceutical loading capacity. In some cases, the encapsulation in these nanovehicles can impart an intestine-targeted and controlled delivery function to encapsulated nutraceuticals. In this paper, the assembly of milk and soy proteins into a variety of nano-architectures, as potential nanovehicles for hydrophobic nutraceuticals is critically reviewed. The strategies to trigger the assembly, or disassembly/reassembly of naturally occurring nano-architectures (e.g., native soy oligomeric globulins and casein micelles), denatured and aggregated proteins (e.g., soy protein isolate and whey protein isolate), and monomeric globular proteins (e.g., β-lactoglobulin) are highlighted. The general principles of protein self-assembly are also discussed. Due to the fast increasing interests for the incorporation of hydrophobic nutraceuticals in many novel food formulations, this review is of relevance for providing a state-of-art knowledge about the strategies and approaches to develop food protein-based nano-architectures as effective nanovehicles for nutraceuticals. [Display omitted] •Food proteins exhibit a great potential in nanoencapsulation of nutraceuticals.•General principles of protein self-assembly are presented.•Soy and milk proteins can form versatile nano-architectures via different strategies.•Strategies to trigger the assembly of soy and milk proteins into nano-architectures are highlighted.•Natural architectures (casein micelles and soy globulins) can perform as nanovehicles for nutraceuticals.
AbstractList Incorporation of hydrophobic and poorly soluble nutraceuticals into food formulations is among the great challenges in food science and pharmaceutical fields. One effective strategy to meet this challenge is to develop a kind of food-compatible nanovehicles for improving water solubility, stability, bioavailability and bioactivities of these nutraceuticals. Many food protein-based nano-architectures, e.g., nanoparticles, nano-complexes, nanogels, nano-micelles, nanofibers or nanotubes, have been demonstrated to perform as outstanding nanovehicles in this regard. They are not only nutritional/digestible, safe, and easy to prepare and handle, but also have high encapsulation performance and nutraceutical loading capacity. In some cases, the encapsulation in these nanovehicles can impart an intestine-targeted and controlled delivery function to encapsulated nutraceuticals. In this paper, the assembly of milk and soy proteins into a variety of nano-architectures, as potential nanovehicles for hydrophobic nutraceuticals is critically reviewed. The strategies to trigger the assembly, or disassembly/reassembly of naturally occurring nano-architectures (e.g., native soy oligomeric globulins and casein micelles), denatured and aggregated proteins (e.g., soy protein isolate and whey protein isolate), and monomeric globular proteins (e.g., β-lactoglobulin) are highlighted. The general principles of protein self-assembly are also discussed. Due to the fast increasing interests for the incorporation of hydrophobic nutraceuticals in many novel food formulations, this review is of relevance for providing a state-of-art knowledge about the strategies and approaches to develop food protein-based nano-architectures as effective nanovehicles for nutraceuticals. [Display omitted] •Food proteins exhibit a great potential in nanoencapsulation of nutraceuticals.•General principles of protein self-assembly are presented.•Soy and milk proteins can form versatile nano-architectures via different strategies.•Strategies to trigger the assembly of soy and milk proteins into nano-architectures are highlighted.•Natural architectures (casein micelles and soy globulins) can perform as nanovehicles for nutraceuticals.
Incorporation of hydrophobic and poorly soluble nutraceuticals into food formulations is among the great challenges in food science and pharmaceutical fields. One effective strategy to meet this challenge is to develop a kind of food-compatible nanovehicles for improving water solubility, stability, bioavailability and bioactivities of these nutraceuticals. Many food protein-based nano-architectures, e.g., nanoparticles, nano-complexes, nanogels, nano-micelles, nanofibers or nanotubes, have been demonstrated to perform as outstanding nanovehicles in this regard. They are not only nutritional/digestible, safe, and easy to prepare and handle, but also have high encapsulation performance and nutraceutical loading capacity. In some cases, the encapsulation in these nanovehicles can impart an intestine-targeted and controlled delivery function to encapsulated nutraceuticals. In this paper, the assembly of milk and soy proteins into a variety of nano-architectures, as potential nanovehicles for hydrophobic nutraceuticals is critically reviewed. The strategies to trigger the assembly, or disassembly/reassembly of naturally occurring nano-architectures (e.g., native soy oligomeric globulins and casein micelles), denatured and aggregated proteins (e.g., soy protein isolate and whey protein isolate), and monomeric globular proteins (e.g., β-lactoglobulin) are highlighted. The general principles of protein self-assembly are also discussed. Due to the fast increasing interests for the incorporation of hydrophobic nutraceuticals in many novel food formulations, this review is of relevance for providing a state-of-art knowledge about the strategies and approaches to develop food protein-based nano-architectures as effective nanovehicles for nutraceuticals.
ArticleNumber 106710
Author Tang, Chuan-He
Author_xml – sequence: 1
  givenname: Chuan-He
  surname: Tang
  fullname: Tang, Chuan-He
  email: chtang@scut.edu.cn
  organization: The Research Group of Food Colloids and Nanotechnology, School of Food Science and Engineering, South China University of Technology, Guangzhou, 510640, China
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Cites_doi 10.1021/jf60217a027
10.1016/0076-6879(86)31045-0
10.1021/bi700091r
10.1016/j.foodchem.2012.11.016
10.1016/j.cis.2017.02.010
10.1016/j.biotechadv.2007.07.006
10.1007/s12393-012-9050-3
10.1016/j.cocis.2009.11.002
10.1016/j.colsurfb.2019.03.051
10.1016/j.foodhyd.2010.03.015
10.1017/S0022029906001725
10.1021/acs.jafc.7b05889
10.1016/S1359-0278(97)00023-0
10.1021/jf300307t
10.1017/S0022029900033306
10.1016/j.foodhyd.2020.106344
10.1146/annurev-food-032818-121907
10.1126/science.1962191
10.1016/j.tifs.2005.12.009
10.1016/j.cocis.2007.07.010
10.1021/jf061417c
10.1016/j.foodres.2014.06.010
10.1016/j.foodhyd.2012.01.016
10.1080/10408398.2015.1067594
10.1039/c2fo10249h
10.1039/C7NR00598A
10.1016/j.foodchem.2018.07.216
10.1016/j.foodhyd.2018.08.031
10.1016/j.foodhyd.2015.11.022
10.1016/j.foodchem.2012.04.020
10.1016/j.foodhyd.2015.12.028
10.1007/s11947-012-0944-0
10.1023/A:1020699200092
10.1016/j.foodhyd.2013.11.010
10.1016/j.foodhyd.2008.10.008
10.1017/S0022029900017295
10.1080/08957959.2011.565057
10.1016/j.colsurfb.2010.06.033
10.1063/1.2951987
10.1021/la900501n
10.1016/j.foodhyd.2014.02.023
10.1016/j.foodres.2020.108979
10.1021/jf201957r
10.1039/b815775h
10.1039/C7FO00812K
10.1038/nbt874
10.1016/j.cocis.2008.01.002
10.1021/acs.nanolett.9b04841
10.1016/j.foodhyd.2019.01.042
10.1016/j.foodhyd.2019.01.012
10.1016/j.foodhyd.2006.09.006
10.1016/j.nantod.2017.04.006
10.1073/pnas.082065899
10.1021/jf400752a
10.1016/S0968-0896(98)00219-3
10.1016/j.foodhyd.2010.11.025
10.1016/j.ijpharm.2017.01.067
10.1016/j.ifset.2011.07.007
10.1039/C4SM00239C
10.1016/j.tifs.2005.12.011
10.1021/acs.jafc.8b05822
10.1016/S0308-8146(01)00099-1
10.1021/jf403847k
10.1080/10408398.2019.1708263
10.1038/nnano.2010.59
10.1021/acs.jafc.8b03798
10.1016/j.sbi.2004.06.006
10.1016/j.idairyj.2010.04.001
10.1016/j.foodhyd.2020.106106
10.1002/(SICI)1097-0282(19981005)46:4<253::AID-BIP7>3.0.CO;2-O
10.1039/C7FO00323D
10.1039/C9FO02035G
10.1016/j.jddst.2020.101531
10.1016/j.foodhyd.2017.03.024
10.1016/j.foodhyd.2017.07.021
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Keywords Nanovehicles
Whey proteins
Casein micelles
Assembly
Soy proteins
Nutraceuticals
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References Menéndez-Aguirre, Kessler, Stuetz, Grune, Weiss, Hinrichs (bib38) 2014; 64
Huppertz, Kelly, de Kruif (bib25) 2006; 73
Shpigelman, Shoham, Israeli-Lev, Livney (bib57) 2014; 40
Lee, Yildiz, dos Santos, Jiang, Andrade, Engeseth (bib30) 2016; 55
Tang (bib62) 2019; 91
Shpigelman, Cohen, Livney (bib55) 2012; 29
Vaia, Smiddy, Kelly, Huppertz (bib68) 2005; 54
Boire, Renard, Bouchoux, Pezennec, Croguennec, Lechevalier (bib4) 2019; 10
Graveland-Bikker, de Kruif (bib19) 2006; 17
Simões, Martíns, Pinheiro, Vicente, Ramos (bib59) 2020; 131
Zhang (bib74) 2003; 21
Ipsen, Otte (bib26) 2007; 25
Kaya-Celiker, Mallikarjunan (bib28) 2012; 4
Simões, Madalena, Pinheiro, Teíxeira, Vicente, Ramos (bib58) 2017; 243
Knoop, Knoop, Wiechen (bib29) 1979; 46
Zimet, Rosenberg, Livney (bib79) 2011; 25
Menéndez-Aguirre, Stuetz, Grune, Kessler, Weiss, Hinrichs (bib39) 2011; 31
Semo, Kesselman, Danino, Livney (bib54) 2007; 21
Ghayour, Hosseini, Eskandari, Esteghlal, Nekoei, Gahruie (bib17) 2019; 87
Pace (bib43) 1986; 131
van der Linden, Venema (bib34) 2007; 12
Chevalier-Lucia, Blayo, Gràcia-Julià, Picart-Palmade, Dumay (bib9) 2011; 12
Hirota-Nakaoka, Goto (bib23) 1999; 7
Hu, Bao, Li, You, Du, Liu (bib24) 2019; 10
Pan, Luo, Gan, Baek, Zhong (bib44) 2014; 10
Schmitt, Bovay, Vuilliomenet, Rouvet, Bovetto, Barbar (bib53) 2009; 25
Li, Li, Bao, Liu, Li, Jiang (bib33) 2017; 9
Wagner, Biliaderis, Moschakis (bib69) 2020
Zhang, Zhou, Zhao, Ning, Sun-Waterhouse, Sun (bib77) 2017; 8
Li, Du, Jin, Du (bib32) 2012; 60
Ron, Zimet, Bargarum, Livney (bib51) 2010; 20
Uversky, Narizhneva, Kirschstein, Winter, Löber (bib67) 1997; 2
O'Mahony, Fox (bib42) 2013
Gögelein, Nägele, Tuinier, Gibaud, Stradner, Schurtenberger (bib18) 2008; 129
Tarhini, Greige-Gerges, Elaissari (bib65) 2017; 522
Ezhilarasi, Karthik, Chhanwal, Anandharamakrishnan (bib16) 2013; 6
Dickinson, Scott, Hussein, Argos, Nielsen (bib14) 1990; 2
Rehan, Ahemad, Gupta (bib48) 2019; 179
Adamcik, Jung, Flakowski, de los Rios, Dietler, Mezzenga (bib2) 2010; 5
Sun, Luo, Hou, Liu (bib60) 2017; 14
Chen, Zhao, Chassenieux, Nicolai (bib8) 2017; 70
Otzen, Sehgal, Nesgaard (bib41) 2007; 46
Shpigelman, Israeli, Livney (bib56) 2010; 24
Wang, Wang, Qian, Wang, Chunyu, Xie (bib70) 1999; 18
Whitesides, Mathias, Seto (bib73) 1991; 254
Zhang, Zhao, Ning, Yu, Tang, Zhou (bib75) 2018; 66
Liu, Liu, Li, Zhang, Tang (bib35) 2019; 67
Chen, Zhao, Chassenieux, Nicolai (bib7) 2016; 56
Pan, Zhong, Baek (bib45) 2013; 61
Sáiz-Abajo, González-Ferrero, Moreno-Ruíz, Romo-Hualde (bib52) 2013; 138
Roach, Harte (bib50) 2008; 9
Tang (bib61) 2017; 57
Du, Bao, Huang, Jiang, Jiao, Ren (bib15) 2019; 271
Jiang, Huang, Bao, Jiao, Zhao, Du (bib27) 2018; 66
Livney (bib37) 2010; 1i5
Relkin, Shukat (bib49) 2012; 134
Dalgleish, Law (bib12) 1988; 55
Dickinson (bib13) 2010; 81
Bao, Liu, Li, Chai, Zhang, Jiao (bib3) 2020; 20
Haham, Ish-Shalom, Nodelman, Duek, Segal, Kustanovich (bib22) 2012; 3
Pérez, David-Birman, Kesselman, Levi-Tal, Lesmes (bib46) 2014; 38
Acosta (bib1) 2009; 14
Grinberg, Grinberg, Burova, Dalgalarrondo, Haertlé (bib21) 1998; 46
Thanh, Shibasaki (bib66) 1978; 26
Zimet, Livney (bib78) 2009; 23
Mohammadian, Moghadam, Salami, Emam-Djomeh, Alavi, Momen (bib40) 2020; 56
Cohen, Levi, Lesmes, Margier, Reboul, Livney (bib10) 2017; 8
Zhang, Zhou, Zhao, Lin, Ning, Sun (bib76) 2018; 74
Chen, Remondetto, Subirade (bib6) 2006; 17
Graveland-Bikker, Koning, Koerten, Geels, Heeren, de Kruif (bib20) 2009; 5
Liang, Tang (bib31) 2013; 61
Rajagopal, Schneider (bib47) 2004; 14
Boulet, Britten, Lamarche (bib5) 2001; 74
Whitesides, Boncheva (bib72) 2002; 99
Tang (bib63) 2020; 109
Wang, Yang, Yin, Zhang, Tang, Li (bib71) 2011; 59
Liu, Li, Zhang, Tang (bib36) 2019; 91
Tang (bib64) 2021; 112
Dalgleish, Law (bib11) 1988; 55
Zimet (10.1016/j.foodhyd.2021.106710_bib78) 2009; 23
Rajagopal (10.1016/j.foodhyd.2021.106710_bib47) 2004; 14
Shpigelman (10.1016/j.foodhyd.2021.106710_bib56) 2010; 24
Acosta (10.1016/j.foodhyd.2021.106710_bib1) 2009; 14
O'Mahony (10.1016/j.foodhyd.2021.106710_bib42) 2013
Ghayour (10.1016/j.foodhyd.2021.106710_bib17) 2019; 87
Schmitt (10.1016/j.foodhyd.2021.106710_bib53) 2009; 25
Graveland-Bikker (10.1016/j.foodhyd.2021.106710_bib20) 2009; 5
Dalgleish (10.1016/j.foodhyd.2021.106710_bib11) 1988; 55
Jiang (10.1016/j.foodhyd.2021.106710_bib27) 2018; 66
Livney (10.1016/j.foodhyd.2021.106710_bib37) 2010; 1i5
Chevalier-Lucia (10.1016/j.foodhyd.2021.106710_bib9) 2011; 12
Vaia (10.1016/j.foodhyd.2021.106710_bib68) 2005; 54
Sun (10.1016/j.foodhyd.2021.106710_bib60) 2017; 14
Whitesides (10.1016/j.foodhyd.2021.106710_bib72) 2002; 99
Shpigelman (10.1016/j.foodhyd.2021.106710_bib55) 2012; 29
Uversky (10.1016/j.foodhyd.2021.106710_bib67) 1997; 2
Ron (10.1016/j.foodhyd.2021.106710_bib51) 2010; 20
Rehan (10.1016/j.foodhyd.2021.106710_bib48) 2019; 179
Cohen (10.1016/j.foodhyd.2021.106710_bib10) 2017; 8
Li (10.1016/j.foodhyd.2021.106710_bib33) 2017; 9
Pace (10.1016/j.foodhyd.2021.106710_bib43) 1986; 131
Chen (10.1016/j.foodhyd.2021.106710_bib6) 2006; 17
Adamcik (10.1016/j.foodhyd.2021.106710_bib2) 2010; 5
Liu (10.1016/j.foodhyd.2021.106710_bib35) 2019; 67
Ezhilarasi (10.1016/j.foodhyd.2021.106710_bib16) 2013; 6
Semo (10.1016/j.foodhyd.2021.106710_bib54) 2007; 21
Tang (10.1016/j.foodhyd.2021.106710_bib62) 2019; 91
Pan (10.1016/j.foodhyd.2021.106710_bib45) 2013; 61
Chen (10.1016/j.foodhyd.2021.106710_bib7) 2016; 56
Du (10.1016/j.foodhyd.2021.106710_bib15) 2019; 271
Simões (10.1016/j.foodhyd.2021.106710_bib58) 2017; 243
Wang (10.1016/j.foodhyd.2021.106710_bib71) 2011; 59
Bao (10.1016/j.foodhyd.2021.106710_bib3) 2020; 20
Tang (10.1016/j.foodhyd.2021.106710_bib63) 2020; 109
Simões (10.1016/j.foodhyd.2021.106710_bib59) 2020; 131
Chen (10.1016/j.foodhyd.2021.106710_bib8) 2017; 70
Wang (10.1016/j.foodhyd.2021.106710_bib70) 1999; 18
Dickinson (10.1016/j.foodhyd.2021.106710_bib13) 2010; 81
Kaya-Celiker (10.1016/j.foodhyd.2021.106710_bib28) 2012; 4
Zhang (10.1016/j.foodhyd.2021.106710_bib77) 2017; 8
Gögelein (10.1016/j.foodhyd.2021.106710_bib18) 2008; 129
Li (10.1016/j.foodhyd.2021.106710_bib32) 2012; 60
Mohammadian (10.1016/j.foodhyd.2021.106710_bib40) 2020; 56
Relkin (10.1016/j.foodhyd.2021.106710_bib49) 2012; 134
Tarhini (10.1016/j.foodhyd.2021.106710_bib65) 2017; 522
Wagner (10.1016/j.foodhyd.2021.106710_bib69) 2020
Grinberg (10.1016/j.foodhyd.2021.106710_bib21) 1998; 46
Menéndez-Aguirre (10.1016/j.foodhyd.2021.106710_bib39) 2011; 31
Boire (10.1016/j.foodhyd.2021.106710_bib4) 2019; 10
Haham (10.1016/j.foodhyd.2021.106710_bib22) 2012; 3
Whitesides (10.1016/j.foodhyd.2021.106710_bib73) 1991; 254
Boulet (10.1016/j.foodhyd.2021.106710_bib5) 2001; 74
Knoop (10.1016/j.foodhyd.2021.106710_bib29) 1979; 46
Sáiz-Abajo (10.1016/j.foodhyd.2021.106710_bib52) 2013; 138
Hu (10.1016/j.foodhyd.2021.106710_bib24) 2019; 10
Tang (10.1016/j.foodhyd.2021.106710_bib64) 2021; 112
Zhang (10.1016/j.foodhyd.2021.106710_bib74) 2003; 21
Zhang (10.1016/j.foodhyd.2021.106710_bib76) 2018; 74
Huppertz (10.1016/j.foodhyd.2021.106710_bib25) 2006; 73
Tang (10.1016/j.foodhyd.2021.106710_bib61) 2017; 57
Ipsen (10.1016/j.foodhyd.2021.106710_bib26) 2007; 25
Liu (10.1016/j.foodhyd.2021.106710_bib36) 2019; 91
Zhang (10.1016/j.foodhyd.2021.106710_bib75) 2018; 66
Shpigelman (10.1016/j.foodhyd.2021.106710_bib57) 2014; 40
Menéndez-Aguirre (10.1016/j.foodhyd.2021.106710_bib38) 2014; 64
Thanh (10.1016/j.foodhyd.2021.106710_bib66) 1978; 26
Dalgleish (10.1016/j.foodhyd.2021.106710_bib12) 1988; 55
van der Linden (10.1016/j.foodhyd.2021.106710_bib34) 2007; 12
Otzen (10.1016/j.foodhyd.2021.106710_bib41) 2007; 46
Lee (10.1016/j.foodhyd.2021.106710_bib30) 2016; 55
Zimet (10.1016/j.foodhyd.2021.106710_bib79) 2011; 25
Liang (10.1016/j.foodhyd.2021.106710_bib31) 2013; 61
Dickinson (10.1016/j.foodhyd.2021.106710_bib14) 1990; 2
Pérez (10.1016/j.foodhyd.2021.106710_bib46) 2014; 38
Hirota-Nakaoka (10.1016/j.foodhyd.2021.106710_bib23) 1999; 7
Graveland-Bikker (10.1016/j.foodhyd.2021.106710_bib19) 2006; 17
Pan (10.1016/j.foodhyd.2021.106710_bib44) 2014; 10
Roach (10.1016/j.foodhyd.2021.106710_bib50) 2008; 9
References_xml – volume: 70
  start-page: 88
  year: 2017
  end-page: 95
  ident: bib8
  article-title: The effect of adding NaCl on the thermal aggregation and gelation of soy protein isolate
  publication-title: Food Hydrocolloids
– volume: 9
  start-page: 9317
  year: 2017
  end-page: 9324
  ident: bib33
  article-title: Bioinspired peptosomes with programmed stimuli-responses for sequential drug release and high-performance anticancer therapy
  publication-title: Nanoscale
– volume: 66
  start-page: 4208
  year: 2018
  end-page: 4218
  ident: bib75
  article-title: Development of a sono-assembled, bifunctional soy peptide nanoparticle for cellular delivery of hydrophobic active cargos
  publication-title: Journal of Agricultural and Food Chemistry
– volume: 2
  start-page: 163
  year: 1997
  end-page: 172
  ident: bib67
  article-title: Conformational transitions provoked by organic solvents in
  publication-title: Folding & Design
– volume: 8
  start-page: 2133
  year: 2017
  end-page: 2141
  ident: bib10
  article-title: Re-assembled casein micelles improve
  publication-title: Food & Function
– volume: 29
  start-page: 57
  year: 2012
  end-page: 67
  ident: bib55
  article-title: Thermally-induced β-lactoglobulin-EGCG nanovehicles: Loading, stability, sensory and digestive-release study
  publication-title: Food Hydrocolloids
– volume: 91
  start-page: 92
  year: 2019
  end-page: 116
  ident: bib62
  article-title: Nanostructured soy proteins: Fabrication and applications as delivery systems for bioactives (a review)
  publication-title: Food Hydrocolloids
– volume: 10
  start-page: 521
  year: 2019
  end-page: 539
  ident: bib4
  article-title: Soft-matter approaches for controlling food protein interactions and assembly
  publication-title: Annual Reviews of Food Science and Technology
– volume: 7
  start-page: 67
  year: 1999
  end-page: 73
  ident: bib23
  article-title: Alcohol-induced denaturation of β-lactoglobulin: A close correlation to the alcohol-induced α-helix formation of melittin
  publication-title: Bioorganic & Medicinal Chemistry
– volume: 66
  start-page: 12921
  year: 2018
  end-page: 12930
  ident: bib27
  article-title: Enzymatically partially hydrolyzed α-lactalbumin peptides for self-assembled micelle formation and their application for coencapsulation of multiple antioxidants
  publication-title: Journal of Agricultural and Food Chemistry
– volume: 25
  start-page: 7899
  year: 2009
  end-page: 7909
  ident: bib53
  article-title: Multiscale characterization of individualized
  publication-title: Langmuir
– volume: 5
  start-page: 423
  year: 2010
  end-page: 428
  ident: bib2
  article-title: Understanding amyloid aggregation by statistical analysis of atomic force microscopy images
  publication-title: Nature Nanotechnology
– volume: 2
  start-page: 403
  year: 1990
  end-page: 413
  ident: bib14
  article-title: Effect of structural modifications on the assembly of a glycinin subunit
  publication-title: The Plant Cell Online
– volume: 9
  start-page: 1
  year: 2008
  end-page: 8
  ident: bib50
  article-title: Disruption and sedimentation of casein micelles and casein micelle isolates under high-pressure homogenization
  publication-title: s
– volume: 46
  start-page: 347
  year: 1979
  end-page: 350
  ident: bib29
  article-title: Sub-structure of synthetic casein micelles
  publication-title: Journal of Dairy Research
– volume: 25
  start-page: 602
  year: 2007
  end-page: 605
  ident: bib26
  article-title: Self-assembly of partially hydrolysated
  publication-title: Biotechnology Advances
– year: 2020
  ident: bib69
  article-title: Whey proteins: Musings on denaturation, aggregate formation and gelation
  publication-title: Critical Reviews in Food Science and Nutrition
– volume: 4
  start-page: 114
  year: 2012
  end-page: 123
  ident: bib28
  article-title: Better nutrients and therapeutics delivery in food through nanotechnology
  publication-title: Food Engineering Reviews
– volume: 14
  start-page: 3
  year: 2009
  end-page: 15
  ident: bib1
  article-title: Bioavailability of nanoparticles in nutrient and nutraceutical delivery
  publication-title: Current Opinion in Colloid & Interface Science
– volume: 1i5
  start-page: 73
  year: 2010
  end-page: 83
  ident: bib37
  article-title: Milk proteins as vehicles for bioactives
  publication-title: Current Opinion in Colloid & Interface Science
– volume: 12
  start-page: 158
  year: 2007
  end-page: 165
  ident: bib34
  article-title: Self-assembly and aggregation of proteins
  publication-title: Current Opinion in Colloid & Interface Science
– volume: 10
  start-page: 8263
  year: 2019
  end-page: 8272
  ident: bib24
  article-title: The construction of enzymolyzed α-lactalbumin based micellar nanoassemblies for encapsulating various kinds of hydrophobic bioactive compounds
  publication-title: Food & Function
– volume: 21
  start-page: 1171
  year: 2003
  end-page: 1178
  ident: bib74
  article-title: Fabrication of novel biomaterials through molecular self-assembly
  publication-title: Nature Biotechnology
– volume: 112
  start-page: 106344
  year: 2021
  ident: bib64
  article-title: Strategies to utilize naturally occurring protein architectures as nanovehicles for hydrophobic nutraceuticals (a review)
  publication-title: Food Hydrocolloids
– volume: 12
  start-page: 416
  year: 2011
  end-page: 425
  ident: bib9
  article-title: Processing of phosphocasein dispersions by dynamic high pressure: Effects on the dispersion physico-chemical characteristics and the binding of
  publication-title: Innovative Food Science & Emerging Technologies
– volume: 3
  start-page: 737
  year: 2012
  end-page: 744
  ident: bib22
  article-title: Stability and bioavailability of vitamin D nanoencapsulated in casein micelles
  publication-title: Food & Function
– volume: 81
  start-page: 130
  year: 2010
  end-page: 140
  ident: bib13
  article-title: Flocculation of protein-stabilized oil-in-water emulsions
  publication-title: Colloids and Surfaces B: Biointerfaces
– volume: 23
  start-page: 1120
  year: 2009
  end-page: 1126
  ident: bib78
  article-title: Beta-lactoglobulin and its nanocomplexes with pectin as vehicles for ω-3 polyunsaturated fatty acids
  publication-title: Food Hydrocolloids
– volume: 55
  start-page: 727
  year: 1988
  end-page: 735
  ident: bib12
  article-title: pH-induced dissociation of bovine casein micelles. II. Mineral solubilization and its relation to casein release
  publication-title: Journal of Dairy Research
– volume: 40
  start-page: 214
  year: 2014
  end-page: 224
  ident: bib57
  article-title: β-Lactoglobulin-naringenin complexes: Nano-vehicles for the delivery of a hydrophobic nutraceutical
  publication-title: Food Hydrocolloids
– volume: 243
  start-page: 23
  year: 2017
  end-page: 45
  ident: bib58
  article-title: Micro- and nano bio-based delivery systems for food applications:
  publication-title: Advances in Colloid and Interface Science
– volume: 31
  start-page: 265
  year: 2011
  end-page: 274
  ident: bib39
  article-title: High pressure-assisted encapsulation of vitamin D
  publication-title: High Pressure Research
– volume: 55
  start-page: 200
  year: 2016
  end-page: 209
  ident: bib30
  article-title: Soy protein nano-aggregates with improved functional properties prepared with sequential pH treatment and ultrasonication
  publication-title: Food Hydrocolloids
– volume: 57
  start-page: 2636
  year: 2017
  end-page: 2679
  ident: bib61
  article-title: Emulsifying properties of soy proteins: A critical review with emphasis on the role of conformational flexibility
  publication-title: Critical Reviews in Food Science and Nutrition
– volume: 18
  start-page: 547
  year: 1999
  end-page: 555
  ident: bib70
  article-title: Methanol-induced unfolding and refolding of cytochrome b5 and its P40V mutant monitored by UV-Visible, CD, and fluorescence spectra
  publication-title: Journal of Protein Chemistry
– volume: 38
  start-page: 40
  year: 2014
  end-page: 47
  ident: bib46
  article-title: Milk protein-vitamin interactions: Formation of beta-lactoglobulin/folid acid nano-complexes and their impact on
  publication-title: Food Hydrocolloids
– volume: 56
  start-page: 417
  year: 2016
  end-page: 424
  ident: bib7
  article-title: Structure of self-assembled native soy globulin in aqueous solution as a function of the concentration and the pH
  publication-title: Food Hydrocolloids
– volume: 10
  start-page: 6820
  year: 2014
  end-page: 6830
  ident: bib44
  article-title: pH-driven encapsulation of curcumin in self-assembled casein nanoparticles for enhanced dispersibility and bioactivity
  publication-title: Soft Matter
– volume: 87
  start-page: 394
  year: 2019
  end-page: 403
  ident: bib17
  article-title: Nanoencapsulation of quercetin and curcumin in casein-based delivery systems
  publication-title: Food Hydrocolloids
– volume: 5
  start-page: 2020
  year: 2009
  end-page: 2026
  ident: bib20
  article-title: Structural characterization of α-lactalbumin nanotubes
  publication-title: Soft Matter
– volume: 74
  start-page: 62
  year: 2018
  end-page: 71
  ident: bib76
  article-title: Soy peptide nanoparticles by ultrasound-induced self-assembly of large peptide aggregates and their role on emulsion stability
  publication-title: Food Hydrocolloids
– volume: 67
  start-page: 6292
  year: 2019
  end-page: 6301
  ident: bib35
  article-title: Novel soy
  publication-title: Journal of Agricultural and Food Chemistry
– volume: 64
  start-page: 74
  year: 2014
  end-page: 80
  ident: bib38
  article-title: Increased loading of vitamin D
  publication-title: Food Research International
– volume: 91
  start-page: 246
  year: 2019
  end-page: 255
  ident: bib36
  article-title: Novel soy
  publication-title: Food Hydrocolloids
– volume: 134
  start-page: 2141
  year: 2012
  end-page: 2148
  ident: bib49
  article-title: Food protein aggregates as vitamin-matrix carriers: Impact of processing conditions
  publication-title: Food Chemistry
– volume: 60
  start-page: 3477
  year: 2012
  end-page: 3484
  ident: bib32
  article-title: Preservation of (-)-epigallocatechin-3-gallate antioxidant properties loaded in heat treated
  publication-title: Journal of Agricultural and Food Chemistry
– volume: 138
  start-page: 1581
  year: 2013
  end-page: 1587
  ident: bib52
  article-title: Thermal protection of
  publication-title: Food Chemistry
– volume: 109
  start-page: 106106
  year: 2020
  ident: bib63
  article-title: Nanocomplexation of proteins with curcumin: From interaction to nanoencapsulation (a reivew)
  publication-title: Food Hydrocolloids
– volume: 46
  start-page: 4348
  year: 2007
  end-page: 4359
  ident: bib41
  article-title: Alternative membrane protein conformations in alcohols
  publication-title: Biochemistry
– volume: 59
  start-page: 7324
  year: 2011
  end-page: 7332
  ident: bib71
  article-title: Structural rearrangement of ethanol-denatured soy proteins by high hydrostatic pressure treatment
  publication-title: Journal of Agricultural and Food Chemistry
– volume: 271
  start-page: 707
  year: 2019
  end-page: 714
  ident: bib15
  article-title: Improved stability, epithelial permeability and cellular antioxidant activity of
  publication-title: Food Chemistry
– volume: 131
  start-page: 108979
  year: 2020
  ident: bib59
  article-title: β-lactoglobulin micro- and nanostructures as bioactive compounds vehicle: In vitro studies
  publication-title: Food Research International
– volume: 74
  start-page: 69
  year: 2001
  end-page: 74
  ident: bib5
  article-title: Dispersion of food proteins in water-alcohol mixed dispersants
  publication-title: Food Chemistry
– volume: 55
  start-page: 529
  year: 1988
  end-page: 538
  ident: bib11
  article-title: pH-induced dissociation of bovine casein micelles. I. Analysis of liberated caseins
  publication-title: Journal of Dairy Research
– volume: 17
  start-page: 196
  year: 2006
  end-page: 203
  ident: bib19
  article-title: Unique milk protein based nanotubes: Food and nanotechnology meet
  publication-title: Trends in Food Science & Technology
– volume: 20
  start-page: 686
  year: 2010
  end-page: 693
  ident: bib51
  article-title: Beta-lactoglobulin-polysaccharide complexes as nanovehicles for hydrophobic nutraceuticals in non-fat foods and clear beverages
  publication-title: International Dairy Journal
– volume: 61
  start-page: 11140
  year: 2013
  end-page: 11150
  ident: bib31
  article-title: Emulsifying and interfacial properties of vicilins: Role of conformational flexibility at quaternary and/or tertiary levels
  publication-title: Journal of Agricultural and Food Chemistry
– volume: 56
  start-page: 101531
  year: 2020
  ident: bib40
  article-title: Whey protein aggregates formed by non-toxic chemical cross-linking as novel carriers for curcumin delivery: Fabrication and characterization
  publication-title: Journal of Drug Delivery Science and Technology
– volume: 73
  start-page: 294
  year: 2006
  end-page: 298
  ident: bib25
  article-title: Disruption and reassociation of casein micelles under high pressure
  publication-title: Journal of Dairy Research
– volume: 522
  start-page: 172
  year: 2017
  end-page: 197
  ident: bib65
  article-title: Protein-based nanoparticles: From preparation to encapsulation of active molecules
  publication-title: International Journal of Pharmaceutics
– volume: 21
  start-page: 936
  year: 2007
  end-page: 942
  ident: bib54
  article-title: Casein micelle as a natural nano-capsular vehicle for nutraceuticals
  publication-title: Food Hydrocolloids
– volume: 25
  start-page: 1270
  year: 2011
  end-page: 1276
  ident: bib79
  article-title: Re-assembled casein micelles and casein nanoparticles as nano-vehicles for
  publication-title: Food Hydrocolloids
– volume: 14
  start-page: 480
  year: 2004
  end-page: 486
  ident: bib47
  article-title: Self-assembling peptides and proteins for nanotechnological applications
  publication-title: Current Opinion in Structural Biology
– volume: 179
  start-page: 280
  year: 2019
  end-page: 292
  ident: bib48
  article-title: Casein nanomicelle as an emerging biomaterial – a comprehensive review
  publication-title: Colloids and Surfaces B: Biointerfaces
– volume: 14
  start-page: 16
  year: 2017
  end-page: 41
  ident: bib60
  article-title: Nanostructures based on protein self-assembly: From hierarchical construction to bioinspired materials
  publication-title: Nano Today
– volume: 8
  start-page: 4384
  year: 2017
  end-page: 4395
  ident: bib77
  article-title: Soy peptide aggregates formed during hydrolysis reduced protein extraction without decreasing their nutritional value
  publication-title: Food & Function
– volume: 61
  start-page: 6036
  year: 2013
  end-page: 6043
  ident: bib45
  article-title: Enhanced dispersibility and bioactivity of curcumin by encapsulation in casein nanocapsules
  publication-title: Journal of Agricultural and Food Chemistry
– volume: 54
  start-page: 8288
  year: 2005
  end-page: 8293
  ident: bib68
  article-title: Solvent-mediated disruption of bovine casein micelles at alkaline pH
  publication-title: Journal of Agricultural and Food Chemistry
– volume: 129
  start-page: 85
  year: 2008
  end-page: 102
  ident: bib18
  article-title: A simple patchy colloid model for the phase behavior of lysozyme dispersions
  publication-title: Journal of Physical Chemistry
– volume: 254
  start-page: 1312
  year: 1991
  ident: bib73
  article-title: Molecular self-assembly and nanochemistry: A chemical strategy for the synthesis of nanostructures
  publication-title: Science
– volume: 17
  start-page: 272
  year: 2006
  end-page: 283
  ident: bib6
  article-title: Food protein-based materials as nutraceutical delivery systems
  publication-title: Trends in Food Science & Technology
– volume: 26
  start-page: 695
  year: 1978
  end-page: 699
  ident: bib66
  article-title: Major proteins of soybean seeds. Reconstitution of
  publication-title: Journal of Agricultural and Food Chemistry
– start-page: 43
  year: 2013
  end-page: 85
  ident: bib42
  article-title: Milk proteins: Introduction and historical aspects
  publication-title: ns: Basic aspects
– volume: 46
  start-page: 253
  year: 1998
  end-page: 265
  ident: bib21
  article-title: Ethanol-induced conformational transitions in Holo-
  publication-title: Biopolymers
– volume: 6
  start-page: 628
  year: 2013
  end-page: 647
  ident: bib16
  article-title: Nanoencapsulation techniques for food bioactive compounds: A review
  publication-title: Food and Bioprocess Technology
– volume: 131
  start-page: 266
  year: 1986
  end-page: 280
  ident: bib43
  article-title: Determination and analysis of urea and guanidine hydrochloride denaturation curves
  publication-title: Methods in Enzymology
– volume: 24
  start-page: 735
  year: 2010
  end-page: 743
  ident: bib56
  article-title: Thermally-induced protein-polyphenol co-assemblies: Beta lactoglobulin-based nanocomplexes as protective nanovehicles for EGCG
  publication-title: Food Hydrocolloids
– volume: 20
  start-page: 1352
  year: 2020
  end-page: 1361
  ident: bib3
  article-title: Enhanced transport of shape and rigidity-tuned
  publication-title: Nano Letters
– volume: 99
  start-page: 4769
  year: 2002
  end-page: 4774
  ident: bib72
  article-title: Beyond molecules: Self-assembly of mesoscopic and macroscopic components
  publication-title: The Proceedings of National Academy Society of the United States of American
– volume: 26
  start-page: 695
  year: 1978
  ident: 10.1016/j.foodhyd.2021.106710_bib66
  article-title: Major proteins of soybean seeds. Reconstitution of β-conglycinin from its subunits
  publication-title: Journal of Agricultural and Food Chemistry
  doi: 10.1021/jf60217a027
– volume: 2
  start-page: 403
  year: 1990
  ident: 10.1016/j.foodhyd.2021.106710_bib14
  article-title: Effect of structural modifications on the assembly of a glycinin subunit
  publication-title: The Plant Cell Online
– volume: 131
  start-page: 266
  year: 1986
  ident: 10.1016/j.foodhyd.2021.106710_bib43
  article-title: Determination and analysis of urea and guanidine hydrochloride denaturation curves
  publication-title: Methods in Enzymology
  doi: 10.1016/0076-6879(86)31045-0
– volume: 46
  start-page: 4348
  year: 2007
  ident: 10.1016/j.foodhyd.2021.106710_bib41
  article-title: Alternative membrane protein conformations in alcohols
  publication-title: Biochemistry
  doi: 10.1021/bi700091r
– volume: 138
  start-page: 1581
  year: 2013
  ident: 10.1016/j.foodhyd.2021.106710_bib52
  article-title: Thermal protection of β-carotene in re-assembled casein micelles during different processing technologies applied in food industry
  publication-title: Food Chemistry
  doi: 10.1016/j.foodchem.2012.11.016
– volume: 243
  start-page: 23
  year: 2017
  ident: 10.1016/j.foodhyd.2021.106710_bib58
  article-title: Micro- and nano bio-based delivery systems for food applications: In vitro behavior
  publication-title: Advances in Colloid and Interface Science
  doi: 10.1016/j.cis.2017.02.010
– volume: 25
  start-page: 602
  year: 2007
  ident: 10.1016/j.foodhyd.2021.106710_bib26
  article-title: Self-assembly of partially hydrolysated α-lactalbumin
  publication-title: Biotechnology Advances
  doi: 10.1016/j.biotechadv.2007.07.006
– volume: 4
  start-page: 114
  year: 2012
  ident: 10.1016/j.foodhyd.2021.106710_bib28
  article-title: Better nutrients and therapeutics delivery in food through nanotechnology
  publication-title: Food Engineering Reviews
  doi: 10.1007/s12393-012-9050-3
– volume: 1i5
  start-page: 73
  year: 2010
  ident: 10.1016/j.foodhyd.2021.106710_bib37
  article-title: Milk proteins as vehicles for bioactives
  publication-title: Current Opinion in Colloid & Interface Science
  doi: 10.1016/j.cocis.2009.11.002
– volume: 179
  start-page: 280
  year: 2019
  ident: 10.1016/j.foodhyd.2021.106710_bib48
  article-title: Casein nanomicelle as an emerging biomaterial – a comprehensive review
  publication-title: Colloids and Surfaces B: Biointerfaces
  doi: 10.1016/j.colsurfb.2019.03.051
– volume: 24
  start-page: 735
  year: 2010
  ident: 10.1016/j.foodhyd.2021.106710_bib56
  article-title: Thermally-induced protein-polyphenol co-assemblies: Beta lactoglobulin-based nanocomplexes as protective nanovehicles for EGCG
  publication-title: Food Hydrocolloids
  doi: 10.1016/j.foodhyd.2010.03.015
– volume: 73
  start-page: 294
  year: 2006
  ident: 10.1016/j.foodhyd.2021.106710_bib25
  article-title: Disruption and reassociation of casein micelles under high pressure
  publication-title: Journal of Dairy Research
  doi: 10.1017/S0022029906001725
– volume: 66
  start-page: 4208
  year: 2018
  ident: 10.1016/j.foodhyd.2021.106710_bib75
  article-title: Development of a sono-assembled, bifunctional soy peptide nanoparticle for cellular delivery of hydrophobic active cargos
  publication-title: Journal of Agricultural and Food Chemistry
  doi: 10.1021/acs.jafc.7b05889
– volume: 9
  start-page: 1
  year: 2008
  ident: 10.1016/j.foodhyd.2021.106710_bib50
  article-title: Disruption and sedimentation of casein micelles and casein micelle isolates under high-pressure homogenization
  publication-title: Innovative Food Science and Technologies
– volume: 2
  start-page: 163
  year: 1997
  ident: 10.1016/j.foodhyd.2021.106710_bib67
  article-title: Conformational transitions provoked by organic solvents in β-lactoglobulin: Can a molten globule like intermediate be induced by the decrease in dielectric constant?
  publication-title: Folding & Design
  doi: 10.1016/S1359-0278(97)00023-0
– volume: 60
  start-page: 3477
  year: 2012
  ident: 10.1016/j.foodhyd.2021.106710_bib32
  article-title: Preservation of (-)-epigallocatechin-3-gallate antioxidant properties loaded in heat treated β-lactoglobulin nanoparticles
  publication-title: Journal of Agricultural and Food Chemistry
  doi: 10.1021/jf300307t
– volume: 55
  start-page: 529
  year: 1988
  ident: 10.1016/j.foodhyd.2021.106710_bib11
  article-title: pH-induced dissociation of bovine casein micelles. I. Analysis of liberated caseins
  publication-title: Journal of Dairy Research
  doi: 10.1017/S0022029900033306
– volume: 112
  start-page: 106344
  year: 2021
  ident: 10.1016/j.foodhyd.2021.106710_bib64
  article-title: Strategies to utilize naturally occurring protein architectures as nanovehicles for hydrophobic nutraceuticals (a review)
  publication-title: Food Hydrocolloids
  doi: 10.1016/j.foodhyd.2020.106344
– volume: 10
  start-page: 521
  year: 2019
  ident: 10.1016/j.foodhyd.2021.106710_bib4
  article-title: Soft-matter approaches for controlling food protein interactions and assembly
  publication-title: Annual Reviews of Food Science and Technology
  doi: 10.1146/annurev-food-032818-121907
– start-page: 43
  year: 2013
  ident: 10.1016/j.foodhyd.2021.106710_bib42
  article-title: Milk proteins: Introduction and historical aspects
– volume: 254
  start-page: 1312
  year: 1991
  ident: 10.1016/j.foodhyd.2021.106710_bib73
  article-title: Molecular self-assembly and nanochemistry: A chemical strategy for the synthesis of nanostructures
  publication-title: Science
  doi: 10.1126/science.1962191
– volume: 17
  start-page: 196
  year: 2006
  ident: 10.1016/j.foodhyd.2021.106710_bib19
  article-title: Unique milk protein based nanotubes: Food and nanotechnology meet
  publication-title: Trends in Food Science & Technology
  doi: 10.1016/j.tifs.2005.12.009
– volume: 12
  start-page: 158
  year: 2007
  ident: 10.1016/j.foodhyd.2021.106710_bib34
  article-title: Self-assembly and aggregation of proteins
  publication-title: Current Opinion in Colloid & Interface Science
  doi: 10.1016/j.cocis.2007.07.010
– volume: 54
  start-page: 8288
  year: 2005
  ident: 10.1016/j.foodhyd.2021.106710_bib68
  article-title: Solvent-mediated disruption of bovine casein micelles at alkaline pH
  publication-title: Journal of Agricultural and Food Chemistry
  doi: 10.1021/jf061417c
– volume: 64
  start-page: 74
  year: 2014
  ident: 10.1016/j.foodhyd.2021.106710_bib38
  article-title: Increased loading of vitamin D2 in reassembled casein micelles with temperature-modulated high pressure treatment
  publication-title: Food Research International
  doi: 10.1016/j.foodres.2014.06.010
– volume: 29
  start-page: 57
  year: 2012
  ident: 10.1016/j.foodhyd.2021.106710_bib55
  article-title: Thermally-induced β-lactoglobulin-EGCG nanovehicles: Loading, stability, sensory and digestive-release study
  publication-title: Food Hydrocolloids
  doi: 10.1016/j.foodhyd.2012.01.016
– volume: 57
  start-page: 2636
  year: 2017
  ident: 10.1016/j.foodhyd.2021.106710_bib61
  article-title: Emulsifying properties of soy proteins: A critical review with emphasis on the role of conformational flexibility
  publication-title: Critical Reviews in Food Science and Nutrition
  doi: 10.1080/10408398.2015.1067594
– volume: 3
  start-page: 737
  year: 2012
  ident: 10.1016/j.foodhyd.2021.106710_bib22
  article-title: Stability and bioavailability of vitamin D nanoencapsulated in casein micelles
  publication-title: Food & Function
  doi: 10.1039/c2fo10249h
– volume: 9
  start-page: 9317
  year: 2017
  ident: 10.1016/j.foodhyd.2021.106710_bib33
  article-title: Bioinspired peptosomes with programmed stimuli-responses for sequential drug release and high-performance anticancer therapy
  publication-title: Nanoscale
  doi: 10.1039/C7NR00598A
– volume: 271
  start-page: 707
  year: 2019
  ident: 10.1016/j.foodhyd.2021.106710_bib15
  article-title: Improved stability, epithelial permeability and cellular antioxidant activity of β-carotene via encapsulation by self-assembled α-lactalbumin micelles
  publication-title: Food Chemistry
  doi: 10.1016/j.foodchem.2018.07.216
– volume: 87
  start-page: 394
  year: 2019
  ident: 10.1016/j.foodhyd.2021.106710_bib17
  article-title: Nanoencapsulation of quercetin and curcumin in casein-based delivery systems
  publication-title: Food Hydrocolloids
  doi: 10.1016/j.foodhyd.2018.08.031
– volume: 55
  start-page: 200
  year: 2016
  ident: 10.1016/j.foodhyd.2021.106710_bib30
  article-title: Soy protein nano-aggregates with improved functional properties prepared with sequential pH treatment and ultrasonication
  publication-title: Food Hydrocolloids
  doi: 10.1016/j.foodhyd.2015.11.022
– volume: 134
  start-page: 2141
  year: 2012
  ident: 10.1016/j.foodhyd.2021.106710_bib49
  article-title: Food protein aggregates as vitamin-matrix carriers: Impact of processing conditions
  publication-title: Food Chemistry
  doi: 10.1016/j.foodchem.2012.04.020
– volume: 56
  start-page: 417
  year: 2016
  ident: 10.1016/j.foodhyd.2021.106710_bib7
  article-title: Structure of self-assembled native soy globulin in aqueous solution as a function of the concentration and the pH
  publication-title: Food Hydrocolloids
  doi: 10.1016/j.foodhyd.2015.12.028
– volume: 6
  start-page: 628
  year: 2013
  ident: 10.1016/j.foodhyd.2021.106710_bib16
  article-title: Nanoencapsulation techniques for food bioactive compounds: A review
  publication-title: Food and Bioprocess Technology
  doi: 10.1007/s11947-012-0944-0
– volume: 18
  start-page: 547
  year: 1999
  ident: 10.1016/j.foodhyd.2021.106710_bib70
  article-title: Methanol-induced unfolding and refolding of cytochrome b5 and its P40V mutant monitored by UV-Visible, CD, and fluorescence spectra
  publication-title: Journal of Protein Chemistry
  doi: 10.1023/A:1020699200092
– volume: 38
  start-page: 40
  year: 2014
  ident: 10.1016/j.foodhyd.2021.106710_bib46
  article-title: Milk protein-vitamin interactions: Formation of beta-lactoglobulin/folid acid nano-complexes and their impact on in vitro gastro-duodenal proteolysis
  publication-title: Food Hydrocolloids
  doi: 10.1016/j.foodhyd.2013.11.010
– volume: 23
  start-page: 1120
  year: 2009
  ident: 10.1016/j.foodhyd.2021.106710_bib78
  article-title: Beta-lactoglobulin and its nanocomplexes with pectin as vehicles for ω-3 polyunsaturated fatty acids
  publication-title: Food Hydrocolloids
  doi: 10.1016/j.foodhyd.2008.10.008
– volume: 46
  start-page: 347
  year: 1979
  ident: 10.1016/j.foodhyd.2021.106710_bib29
  article-title: Sub-structure of synthetic casein micelles
  publication-title: Journal of Dairy Research
  doi: 10.1017/S0022029900017295
– volume: 31
  start-page: 265
  year: 2011
  ident: 10.1016/j.foodhyd.2021.106710_bib39
  article-title: High pressure-assisted encapsulation of vitamin D2 in reassembled casein micelles
  publication-title: High Pressure Research
  doi: 10.1080/08957959.2011.565057
– volume: 81
  start-page: 130
  year: 2010
  ident: 10.1016/j.foodhyd.2021.106710_bib13
  article-title: Flocculation of protein-stabilized oil-in-water emulsions
  publication-title: Colloids and Surfaces B: Biointerfaces
  doi: 10.1016/j.colsurfb.2010.06.033
– volume: 129
  start-page: 85
  year: 2008
  ident: 10.1016/j.foodhyd.2021.106710_bib18
  article-title: A simple patchy colloid model for the phase behavior of lysozyme dispersions
  publication-title: Journal of Physical Chemistry
  doi: 10.1063/1.2951987
– volume: 25
  start-page: 7899
  year: 2009
  ident: 10.1016/j.foodhyd.2021.106710_bib53
  article-title: Multiscale characterization of individualized β-lactoglobulin microgels formed upon heat treatment under narrow pH range conditions
  publication-title: Langmuir
  doi: 10.1021/la900501n
– volume: 40
  start-page: 214
  year: 2014
  ident: 10.1016/j.foodhyd.2021.106710_bib57
  article-title: β-Lactoglobulin-naringenin complexes: Nano-vehicles for the delivery of a hydrophobic nutraceutical
  publication-title: Food Hydrocolloids
  doi: 10.1016/j.foodhyd.2014.02.023
– volume: 131
  start-page: 108979
  year: 2020
  ident: 10.1016/j.foodhyd.2021.106710_bib59
  article-title: β-lactoglobulin micro- and nanostructures as bioactive compounds vehicle: In vitro studies
  publication-title: Food Research International
  doi: 10.1016/j.foodres.2020.108979
– volume: 55
  start-page: 727
  year: 1988
  ident: 10.1016/j.foodhyd.2021.106710_bib12
  article-title: pH-induced dissociation of bovine casein micelles. II. Mineral solubilization and its relation to casein release
  publication-title: Journal of Dairy Research
  doi: 10.1017/S0022029900033306
– volume: 59
  start-page: 7324
  year: 2011
  ident: 10.1016/j.foodhyd.2021.106710_bib71
  article-title: Structural rearrangement of ethanol-denatured soy proteins by high hydrostatic pressure treatment
  publication-title: Journal of Agricultural and Food Chemistry
  doi: 10.1021/jf201957r
– volume: 5
  start-page: 2020
  year: 2009
  ident: 10.1016/j.foodhyd.2021.106710_bib20
  article-title: Structural characterization of α-lactalbumin nanotubes
  publication-title: Soft Matter
  doi: 10.1039/b815775h
– volume: 8
  start-page: 4384
  year: 2017
  ident: 10.1016/j.foodhyd.2021.106710_bib77
  article-title: Soy peptide aggregates formed during hydrolysis reduced protein extraction without decreasing their nutritional value
  publication-title: Food & Function
  doi: 10.1039/C7FO00812K
– volume: 21
  start-page: 1171
  year: 2003
  ident: 10.1016/j.foodhyd.2021.106710_bib74
  article-title: Fabrication of novel biomaterials through molecular self-assembly
  publication-title: Nature Biotechnology
  doi: 10.1038/nbt874
– volume: 14
  start-page: 3
  year: 2009
  ident: 10.1016/j.foodhyd.2021.106710_bib1
  article-title: Bioavailability of nanoparticles in nutrient and nutraceutical delivery
  publication-title: Current Opinion in Colloid & Interface Science
  doi: 10.1016/j.cocis.2008.01.002
– volume: 20
  start-page: 1352
  year: 2020
  ident: 10.1016/j.foodhyd.2021.106710_bib3
  article-title: Enhanced transport of shape and rigidity-tuned α-lactalbumin nanotubes across intestinal mucus and cellular barriers
  publication-title: Nano Letters
  doi: 10.1021/acs.nanolett.9b04841
– volume: 91
  start-page: 246
  year: 2019
  ident: 10.1016/j.foodhyd.2021.106710_bib36
  article-title: Novel soy β-conglycinin nanoparticles by ethanol-assisted disassembly and reassembly: Outstanding nanocarriers for hydrophobic nutraceuticals
  publication-title: Food Hydrocolloids
  doi: 10.1016/j.foodhyd.2019.01.042
– volume: 91
  start-page: 92
  year: 2019
  ident: 10.1016/j.foodhyd.2021.106710_bib62
  article-title: Nanostructured soy proteins: Fabrication and applications as delivery systems for bioactives (a review)
  publication-title: Food Hydrocolloids
  doi: 10.1016/j.foodhyd.2019.01.012
– volume: 21
  start-page: 936
  year: 2007
  ident: 10.1016/j.foodhyd.2021.106710_bib54
  article-title: Casein micelle as a natural nano-capsular vehicle for nutraceuticals
  publication-title: Food Hydrocolloids
  doi: 10.1016/j.foodhyd.2006.09.006
– volume: 14
  start-page: 16
  year: 2017
  ident: 10.1016/j.foodhyd.2021.106710_bib60
  article-title: Nanostructures based on protein self-assembly: From hierarchical construction to bioinspired materials
  publication-title: Nano Today
  doi: 10.1016/j.nantod.2017.04.006
– volume: 99
  start-page: 4769
  year: 2002
  ident: 10.1016/j.foodhyd.2021.106710_bib72
  article-title: Beyond molecules: Self-assembly of mesoscopic and macroscopic components
  publication-title: The Proceedings of National Academy Society of the United States of American
  doi: 10.1073/pnas.082065899
– volume: 61
  start-page: 6036
  year: 2013
  ident: 10.1016/j.foodhyd.2021.106710_bib45
  article-title: Enhanced dispersibility and bioactivity of curcumin by encapsulation in casein nanocapsules
  publication-title: Journal of Agricultural and Food Chemistry
  doi: 10.1021/jf400752a
– volume: 7
  start-page: 67
  year: 1999
  ident: 10.1016/j.foodhyd.2021.106710_bib23
  article-title: Alcohol-induced denaturation of β-lactoglobulin: A close correlation to the alcohol-induced α-helix formation of melittin
  publication-title: Bioorganic & Medicinal Chemistry
  doi: 10.1016/S0968-0896(98)00219-3
– volume: 25
  start-page: 1270
  year: 2011
  ident: 10.1016/j.foodhyd.2021.106710_bib79
  article-title: Re-assembled casein micelles and casein nanoparticles as nano-vehicles for ω-3 polyunsaturated fatty acids
  publication-title: Food Hydrocolloids
  doi: 10.1016/j.foodhyd.2010.11.025
– volume: 522
  start-page: 172
  year: 2017
  ident: 10.1016/j.foodhyd.2021.106710_bib65
  article-title: Protein-based nanoparticles: From preparation to encapsulation of active molecules
  publication-title: International Journal of Pharmaceutics
  doi: 10.1016/j.ijpharm.2017.01.067
– volume: 12
  start-page: 416
  year: 2011
  ident: 10.1016/j.foodhyd.2021.106710_bib9
  article-title: Processing of phosphocasein dispersions by dynamic high pressure: Effects on the dispersion physico-chemical characteristics and the binding of α-tocopherol acetate to casein micelles
  publication-title: Innovative Food Science & Emerging Technologies
  doi: 10.1016/j.ifset.2011.07.007
– volume: 10
  start-page: 6820
  year: 2014
  ident: 10.1016/j.foodhyd.2021.106710_bib44
  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: 17
  start-page: 272
  year: 2006
  ident: 10.1016/j.foodhyd.2021.106710_bib6
  article-title: Food protein-based materials as nutraceutical delivery systems
  publication-title: Trends in Food Science & Technology
  doi: 10.1016/j.tifs.2005.12.011
– volume: 67
  start-page: 6292
  year: 2019
  ident: 10.1016/j.foodhyd.2021.106710_bib35
  article-title: Novel soy β-conglycinin ‘core-shell’ nanoparticles as outstanding eco-friendly nanocarriers for curcumin
  publication-title: Journal of Agricultural and Food Chemistry
  doi: 10.1021/acs.jafc.8b05822
– volume: 74
  start-page: 69
  year: 2001
  ident: 10.1016/j.foodhyd.2021.106710_bib5
  article-title: Dispersion of food proteins in water-alcohol mixed dispersants
  publication-title: Food Chemistry
  doi: 10.1016/S0308-8146(01)00099-1
– volume: 61
  start-page: 11140
  issue: 46
  year: 2013
  ident: 10.1016/j.foodhyd.2021.106710_bib31
  article-title: Emulsifying and interfacial properties of vicilins: Role of conformational flexibility at quaternary and/or tertiary levels
  publication-title: Journal of Agricultural and Food Chemistry
  doi: 10.1021/jf403847k
– year: 2020
  ident: 10.1016/j.foodhyd.2021.106710_bib69
  article-title: Whey proteins: Musings on denaturation, aggregate formation and gelation
  publication-title: Critical Reviews in Food Science and Nutrition
  doi: 10.1080/10408398.2019.1708263
– volume: 5
  start-page: 423
  year: 2010
  ident: 10.1016/j.foodhyd.2021.106710_bib2
  article-title: Understanding amyloid aggregation by statistical analysis of atomic force microscopy images
  publication-title: Nature Nanotechnology
  doi: 10.1038/nnano.2010.59
– volume: 66
  start-page: 12921
  year: 2018
  ident: 10.1016/j.foodhyd.2021.106710_bib27
  article-title: Enzymatically partially hydrolyzed α-lactalbumin peptides for self-assembled micelle formation and their application for coencapsulation of multiple antioxidants
  publication-title: Journal of Agricultural and Food Chemistry
  doi: 10.1021/acs.jafc.8b03798
– volume: 14
  start-page: 480
  year: 2004
  ident: 10.1016/j.foodhyd.2021.106710_bib47
  article-title: Self-assembling peptides and proteins for nanotechnological applications
  publication-title: Current Opinion in Structural Biology
  doi: 10.1016/j.sbi.2004.06.006
– volume: 20
  start-page: 686
  year: 2010
  ident: 10.1016/j.foodhyd.2021.106710_bib51
  article-title: Beta-lactoglobulin-polysaccharide complexes as nanovehicles for hydrophobic nutraceuticals in non-fat foods and clear beverages
  publication-title: International Dairy Journal
  doi: 10.1016/j.idairyj.2010.04.001
– volume: 109
  start-page: 106106
  year: 2020
  ident: 10.1016/j.foodhyd.2021.106710_bib63
  article-title: Nanocomplexation of proteins with curcumin: From interaction to nanoencapsulation (a reivew)
  publication-title: Food Hydrocolloids
  doi: 10.1016/j.foodhyd.2020.106106
– volume: 46
  start-page: 253
  year: 1998
  ident: 10.1016/j.foodhyd.2021.106710_bib21
  article-title: Ethanol-induced conformational transitions in Holo-α-lactalbumin: Spectral and calorimetric studies
  publication-title: Biopolymers
  doi: 10.1002/(SICI)1097-0282(19981005)46:4<253::AID-BIP7>3.0.CO;2-O
– volume: 8
  start-page: 2133
  year: 2017
  ident: 10.1016/j.foodhyd.2021.106710_bib10
  article-title: Re-assembled casein micelles improve in vitro bioavailability of vitamin D in a Caco-2 cell model
  publication-title: Food & Function
  doi: 10.1039/C7FO00323D
– volume: 10
  start-page: 8263
  year: 2019
  ident: 10.1016/j.foodhyd.2021.106710_bib24
  article-title: The construction of enzymolyzed α-lactalbumin based micellar nanoassemblies for encapsulating various kinds of hydrophobic bioactive compounds
  publication-title: Food & Function
  doi: 10.1039/C9FO02035G
– volume: 56
  start-page: 101531
  year: 2020
  ident: 10.1016/j.foodhyd.2021.106710_bib40
  article-title: Whey protein aggregates formed by non-toxic chemical cross-linking as novel carriers for curcumin delivery: Fabrication and characterization
  publication-title: Journal of Drug Delivery Science and Technology
  doi: 10.1016/j.jddst.2020.101531
– volume: 70
  start-page: 88
  year: 2017
  ident: 10.1016/j.foodhyd.2021.106710_bib8
  article-title: The effect of adding NaCl on the thermal aggregation and gelation of soy protein isolate
  publication-title: Food Hydrocolloids
  doi: 10.1016/j.foodhyd.2017.03.024
– volume: 74
  start-page: 62
  year: 2018
  ident: 10.1016/j.foodhyd.2021.106710_bib76
  article-title: Soy peptide nanoparticles by ultrasound-induced self-assembly of large peptide aggregates and their role on emulsion stability
  publication-title: Food Hydrocolloids
  doi: 10.1016/j.foodhyd.2017.07.021
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Snippet Incorporation of hydrophobic and poorly soluble nutraceuticals into food formulations is among the great challenges in food science and pharmaceutical fields....
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StartPage 106710
SubjectTerms Assembly
bioavailability
casein
Casein micelles
dietary supplements
encapsulation
hydrocolloids
hydrophobicity
micelles
milk
nanofibers
nanogels
nanotubes
Nanovehicles
novel foods
Nutraceuticals
soy protein isolate
Soy proteins
water solubility
whey protein isolate
Whey proteins
Title Assembly of food proteins for nano- encapsulation and delivery of nutraceuticals (a mini-review)
URI https://dx.doi.org/10.1016/j.foodhyd.2021.106710
https://www.proquest.com/docview/2524263342
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