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Food Science and Human Wellness 2020, 9(3): 199-213 https://doi.org/10.1016/j.fshw.2020.04.009
Review Article | Open Access | Issue | Published: 11 May 2020

Nanostructured food proteins as efficient systems for the encapsulation of bioactive compounds

Show Author's Information Mehdi Mohammadiana,  Mostafa I. Walyb,  Maryam Moghadama,  Zahra Emam-Djomeha( ),  Maryam Salamia,  Ali Akbar Moosavi-Movahedic
Department of Food Science and Engineering, University College of Agriculture & Natural Resources, University of Tehran, Karaj, Iran
Department of Food Science and Nutrition, College of Agricultural and Marine Sciences, Sultan Qaboos University, Muscat, Oman
Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran
Keywords:
Nanocarriers, Bioactive compounds, Food proteins, Nanoencapsulation, Release properties
Cite this article:
Mohammadian M, Waly MI, Moghadam M, et al. Nanostructured food proteins as efficient systems for the encapsulation of bioactive compounds. Food Science and Human Wellness, 2020, 9(3): 199-213. https://doi.org/10.1016/j.fshw.2020.04.009
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Abstract Full text About this article

Recently, nanoencapsulation was introduced as an efficient and promising approach for the protection, delivery, and site-specific liberation of the nutraceuticals and bioactive ingredients. Food proteins are attractive materials for developing nanocarriers to protect and deliver bioactives due to their unique functional and biological properties. Food proteins extracted from animals and plants have the ability to form different nanostructures including nanoparticles, hollow particles, nanogels, nanofibrillar aggregates, electrospun nanofibers, nanotubular structures, and nanocomplexes. These nanostructured food proteins have been widely used as nanocarriers for the biologically active compounds and drugs. The release of bioactive compounds from nanocarriers depends mainly on pH as well as swelling and the degradation behavior of nanostructure in the simulated physiological conditions. This review presents the applications of the nanostructured food proteins for the encapsulation of bioactive compounds. The major techniques for the fabrication of nanocarriers are described. The encapsulation, protection, and release of bioactive compounds in different nanostructured food proteins were also discussed.


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About this article

Nanostructured food proteins as efficient systems for the encapsulation of bioactive compounds

Show Author's information Mehdi Mohammadiana, Mostafa I. Walyb, Maryam Moghadama, Zahra Emam-Djomeha( ), Maryam Salamia, Ali Akbar Moosavi-Movahedic
Department of Food Science and Engineering, University College of Agriculture & Natural Resources, University of Tehran, Karaj, Iran
Department of Food Science and Nutrition, College of Agricultural and Marine Sciences, Sultan Qaboos University, Muscat, Oman
Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran

Abstract

Recently, nanoencapsulation was introduced as an efficient and promising approach for the protection, delivery, and site-specific liberation of the nutraceuticals and bioactive ingredients. Food proteins are attractive materials for developing nanocarriers to protect and deliver bioactives due to their unique functional and biological properties. Food proteins extracted from animals and plants have the ability to form different nanostructures including nanoparticles, hollow particles, nanogels, nanofibrillar aggregates, electrospun nanofibers, nanotubular structures, and nanocomplexes. These nanostructured food proteins have been widely used as nanocarriers for the biologically active compounds and drugs. The release of bioactive compounds from nanocarriers depends mainly on pH as well as swelling and the degradation behavior of nanostructure in the simulated physiological conditions. This review presents the applications of the nanostructured food proteins for the encapsulation of bioactive compounds. The major techniques for the fabrication of nanocarriers are described. The encapsulation, protection, and release of bioactive compounds in different nanostructured food proteins were also discussed.

Keywords: Nanocarriers, Bioactive compounds, Food proteins, Nanoencapsulation, Release properties

References(129)

[1]

E. Betoret, N. Betoret, D. Vidal, et al., Functional foods development: trends and technologies, Trends Food Sci. Technol. 22 (2011) 498-508, http://doi.org/10.1016/j.tifs.2011.05.004.
DOI Google Scholar
[2]

A. Madadlou, S. Jaberipour, M.H. Eskandari, Nanoparticulation of enzymatically cross-linked whey proteins to encapsulate caffeine via microemulsification/heat gelation procedure, LWT-Food Sci. Technol. 57 (2014) 725-730, http://doi.org/10.1016/j.lwt.2014.02.041.
DOI Google Scholar
[3]

L. Bagheri, A. Madadlou, M. Yarmand, et al., Nanoencapsulation of date palm pit extract in whey protein particles generated via desolvation method, Food Res. Int. 51 (2013) 866-871, http://doi.org/10.1016/j.foodres.2013.01.058.
DOI Google Scholar
[4]

G.H. Shin, J.T. Kim, H.J. Park, Recent developments in nanoformulations of lipophilic functional foods, Trends Food Sci. Technol. 46 (2015) 144-157, http://doi.org/10.1016/j.tifs.2015.07.005.
DOI Google Scholar
[5]

A. Abaee, M. Mohammadian, S.M. Jafari, Whey and soy protein-based hydrogels and nano-hydrogels as bioactive delivery systems, Trends Food Sci. Technol. 70 (2017) 69-81, http://doi.org/10.1016/j.tifs.2017.10.011.
DOI Google Scholar
[6]

H. Xu, L. Shen, L. Xu, et al., Controlled delivery of hollow corn protein nanoparticles via non-toxic crosslinking: in vivo and drug loading study, Biomed. Microdevices 17 (2015) 1-8, http://doi.org/10.1007/s10544-014-9926-5.
DOI Google Scholar
[7]

O.L. Ramos, R.N. Pereira, A. Martins, et al., Design of whey protein nanostructures for incorporation and release of nutraceutical compounds in food, Crit. Rev. Food Sci. Nutr. 57 (2017) 1377-1393, http://doi.org/10.1080/10408398.2014.993749.
DOI Google Scholar
[8]

M. Fathi, F. Donsi, D.J. McClements, Protein‐based delivery systems for the nanoencapsulation of food ingredients, Compr. Rev. Food Sci. Food Saf. 17 (2018) 920-936, http://doi.org/10.1111/1541-4337.12360.
DOI Google Scholar
[9]

W. Lohcharoenkal, L. Wang, Y.C. Chen, et al., Protein nanoparticles as drug delivery carriers for cancer therapy, Biomed Res. Int. 2014 (2014) 1-12, http://doi.org/10.1155/2014/180549.
DOI Google Scholar
[10]

D. Verma, N. Gulati, S. Kaul, S. Mukherjee, U. Nagaich, Protein based nanostructures for drug delivery, J. Pharm. 2018 (2018) 1-18, http://doi.org/10.1155/2018/9285854.
DOI Google Scholar
[11]

A.O. Elzoghby, W.M. Samy, N.A. Elgindy, Protein-based nanocarriers as promising drug and gene delivery systems, J. Control. Release 161 (2012) 38-49, http://doi.org/10.1016/j.jconrel.2012.04.036.
DOI Google Scholar
[12]

L. Chen, G.E. Remondetto, M. Subirade, Food protein-based materials as nutraceutical delivery systems, Trends Food Sci. Technol. 17 (2006) 272-283, http://doi.org/10.1016/j.tifs.2005.12.011.
DOI Google Scholar
[13]

M. Tarhini, H. Greige-Gerges, A. Elaissari, Protein-based nanoparticles: from preparation to encapsulation of active molecules, Int. J. Pharm. 522 (2017) 172-197, http://doi.org/10.1016/j.ijpharm.2017.01.067.
DOI Google Scholar
[14]

A. Abbasi, Z. Emam-Djomeh, M.A.E. Mousavi, et al., Stability of vitamin D3 encapsulated in nanoparticles of whey protein isolate, Food Chem. 143 (2014) 379-383, http://doi.org/10.1016/j.foodchem.2013.08.018.
DOI Google Scholar
[15]

A. Jain, G. Sharma, G. Ghoshal, et al., Lycopene loaded whey protein isolate nanoparticles: an innovative endeavor for enhanced bioavailability of lycopene and anti-cancer activity, Int. J. Pharm. 546 (2018) 97-105, http://doi.org/10.1016/j.ijpharm.2018.04.061.
DOI Google Scholar
[16]

H. Nourbakhsh, A. Madadlou, Z. Emam-Djomeh, et al., One-pot nanoparticulation of potentially bioactive peptides and gallic acid encapsulation, Food Chem. 210 (2016) 317-324, http://doi.org/10.1016/j.foodchem.2016.04.112.
DOI Google Scholar
[17]

R. Fang, R. Hao, X. Wu, et al., Bovine serum albumin nanoparticle promotes the stability of quercetin in simulated intestinal fluid, J. Agric. Food Chem. 59 (2011) 6292-6298, http://doi.org/10.1021/jf200718j.
DOI Google Scholar
[18]

R. Sadeghi, A.A. Moosavi-Movahedi, Z. Emam-Jomeh, et al., The effect of different desolvating agents on BSA nanoparticle properties and encapsulation of curcumin, J. Nanopart. Res. 16 (2014) 2565-2579, http://doi.org/10.1007/s11051-014-2565-1.
DOI Google Scholar
[19]

Z. Yu, M. Yu, Z. Zhang, et al., Bovine serum albumin nanoparticles as controlled release carrier for local drug delivery to the inner ear, Nanoscale Res. Lett. 9 (2014) 343-350, http://doi.org/10.1186/1556-276X-9-343.
DOI Google Scholar
[20]

Z. Teng, Y. Luo, Q. Wang, Nanoparticles synthesized from soy protein: preparation, characterization, and application for nutraceutical encapsulation, J. Agric. Food Chem. 60 (2012) 2712-2720, http://doi.org/10.1021/jf205238x.
DOI Google Scholar
[21]

J. Zhang, C.J. Field, D. Vine, et al., Intestinal uptake and transport of vitamin B12-loaded soy protein nanoparticles, Pharm. Res. 32 (2015) 1288-1303, http://doi.org/10.1007/s11095-014-1533-x.
DOI Google Scholar
[22]

X. Cheng, X. Wang, Z. Cao, et al., Folic acid-modified soy protein nanoparticles for enhanced targeting and inhibitory, Mater. Sci. Eng. C 71 (2017) 298-307, http://doi.org/10.1016/j.msec.2016.10.018.
DOI Google Scholar
[23]

D.A. Delfiya, K. Thangavel, D. Amirtham, Preparation of curcumin loaded egg albumin nanoparticles using acetone and optimization of desolvation process, Protein J. 35 (2016) 124-135, http://doi.org/10.1007/s10930-016-9652-3.
DOI Google Scholar
[24]

Y. Fan, Y. Liu, L. Gao, et al., Improved chemical stability and cellular antioxidant activity of resveratrol in zein nanoparticle with bovine serum albumin-caffeic acid conjugate, Food Chem. 261 (2018) 283-291, http://doi.org/10.1016/j.foodchem.2018.04.055.
DOI Google Scholar
[25]

F. Dong, X. Dong, L. Zhou, et al., Doxorubicin-loaded biodegradable self-assembly zein nanoparticle and its anti-cancer effect: preparation, in vitro evaluation, and cellular uptake, Colloids Surf. B Biointerfaces 140 (2016) 324-331, http://doi.org/10.1016/j.colsurfb.2015.12.048.
DOI Google Scholar
[26]

M. Jahanshahi, Z. Babaei, Protein nanoparticle: a unique system as drug delivery vehicles, Afr. J. Biotechnol. 7 (2008) 4926-4934, http://doi.org/10.4314/ajb.v7i25.59701.
DOI Google Scholar
[27]

X. Wang, J.I. Feng, Y. Bai, et al., Synthesis, properties, and applications of hollow micro-/nanostructures, Chem. Rev. 116 (2016) 10983-11060, http://doi.org/10.1021/acs.chemrev.5b00731.
DOI Google Scholar
[28]

X.W.D. Lou, L.A. Archer, Z. Yang, Hollow micro‐/nanostructures: synthesis and applications, Adv. Mater. 20 (2008) 3987-4019, http://doi.org/10.1002/adma.200800854.
DOI Google Scholar
[29]

S. Hu, T. Wang, M.L. Fernandez, et al., Development of tannic acid cross-linked hollow zein nanoparticles as potential oral delivery vehicles for curcumin, Food Hydrocoll. 61 (2016) 821-831, http://doi.org/10.1016/j.foodhyd.2016.07.006.
DOI Google Scholar
[30]

H. Xu, Q. Jiang, N. Reddy, et al., Hollow nanoparticles from zein for potential medical applications, J. Mater. Chem. 21 (2011) 18227-18235, http://doi.org/10.1039/C1JM11163A.
DOI Google Scholar
[31]

H. Xu, Y. Zhang, Q. Jiang, et al., Biodegradable hollow zein nanoparticles for removal of reactive dyes from wastewater, J. Environ. Manage. 125 (2013) 33-40, http://doi.org/10.1016/j.jenvman.2013.03.050.
DOI Google Scholar
[32]

C. Liu, W. Yao, L. Zhang, et al., Cell-penetrating hollow spheres based on milk protein, Chem. Comm. 46 (2010) 7566-7568, http://doi.org/10.1039/c0cc02370a.
DOI Google Scholar
[33]

H. Kraskiewicz, B. Breen, T. Sargeant, et al., Assembly of protein-based hollow spheres encapsulating a therapeutic factor, ACS Chem. Neurosci. 4 (2013) 1297-1304, http://doi.org/10.1021/cn400080h.
DOI Google Scholar
[34]

H. Zhang, Y. Zhai, J. Wang, et al., New progress and prospects: the application of nanogel in drug delivery, Mater. Sci. Eng. C 60 (2016) 560-568, http://doi.org/10.1016/j.msec.2015.11.041.
DOI Google Scholar
[35]

K.S. Soni, S.S. Desale, T.K. Bronich, Nanogels: an overview of properties, biomedical applications and obstacles to clinical translation, J. Control. Release 240 (2016) 109-126, http://doi.org/10.1016/j.jconrel.2015.11.009.
DOI Google Scholar
[36]

Y. Akiyama, T. Fujiwara, S.I. Takeda, et al., Preparation of stimuli-responsive protein nanogel by quantum-ray irradiation, Colloid Polym. Sci. 285 (2007) 801-807, http://doi.org/10.1007/s00396-006-1628-y.
DOI Google Scholar
[37]

B. Jin, X. Zhou, X. Li, et al., Self-assembled modified soy protein/dextran nanogel induced by ultrasonication as a delivery vehicle for riboflavin, Molecules 21 (2016) 1-14, http://doi.org/10.3390/molecules21030282.
DOI Google Scholar
[38]

N. Chen, L. Lin, W. Sun, et al., Stable and pH-sensitive protein nanogels made by self-assembly of heat denatured soy protein, J. Agric. Food Chem. 62 (2014) 9553-9561, http://doi.org/10.1021/jf502572d.
DOI Google Scholar
[39]

J.L. Feng, J.R. Qi, S.W. Yin, et al., Fabrication and characterization of stable soy β-conglycinin–dextran core–shell nanogels prepared via a self-assembly approach at the isoelectric point, J. Agric. Food Chem. 63 (2015) 6075-6083, http://doi.org/10.1021/acs.jafc.5b01778.
DOI Google Scholar
[40]

T. Huppertz, C.G. de Kruif, Structure and stability of nanogel particles prepared by internal cross-linking of casein micelles, Int. Dairy J. 18 (2008) 556-565, http://doi.org/10.1016/j.idairyj.2007.10.009.
DOI Google Scholar
[41]

J. Feng, S. Wu, H. Wang, et al., Improved bioavailability of curcumin in ovalbumin-dextran nanogels prepared by Maillard reaction, J. Funct. Foods 27 (2016) 55-68, http://doi.org/10.1016/j.jff.2016.09.002.
DOI Google Scholar
[42]

Z. Li, W. Xu, C. Zhang, et al., Self-assembled lysozyme/carboxymethylcellulose nanogels for delivery of methotrexate, Int. J. Biol. Macromol. 75 (2015) 166-172, http://doi.org/10.1016/j.ijbiomac.2015.01.033.
DOI Google Scholar
[43]

K. Zhu, T. Ye, J. Liu, et al., Nanogels fabricated by lysozyme and sodium carboxymethyl cellulose for 5-fluorouracil controlled release, Int. J. Pharm. 441 (2013) 721-727, http://doi.org/10.1016/j.ijpharm.2012.10.022.
DOI Google Scholar
[44]

L. Lin, W. Xu, H. Liang, et al., Construction of pH-sensitive lysozyme/pectin nanogel for tumor methotrexate delivery, Colloids Surf. B Biointerfaces 126 (2015) 459-466, http://doi.org/10.1016/j.colsurfb.2014.12.051.
DOI Google Scholar
[45]

A.I. Bourbon, M.A. Cerqueira, A.A. Vicente, Encapsulation and controlled release of bioactive compounds in lactoferrin-glycomacropeptide nanohydrogels: curcumin and caffeine as model compounds, J. Food Eng. 180 (2016) 110-119, http://doi.org/10.1016/j.jfoodeng.2016.02.016.
DOI Google Scholar
[46]

A.I. Bourbon, A.C. Pinheiro, M.A. Cerqueira, et al., Influence of chitosan coating on protein-based nanohydrogels properties and in vitro gastric digestibility, Food Hydrocoll. 60 (2016) 109-118, http://doi.org/10.1016/j.foodhyd.2016.03.002.
DOI Google Scholar
[47]

A.I. Bourbon, A.C. Pinheiro, M.G. Carneiro-da-Cunha, et al., Development and characterization of lactoferrin-GMP nanohydrogels: evaluation of pH, ionic strength and temperature effect, Food Hydrocoll. 48 (2015) 292-300, http://doi.org/10.1016/j.foodhyd.2015.02.026.
DOI Google Scholar
[48]

Y. Wang, S. Xu, W. Xiong, et al., Nanogels fabricated from bovine serum albumin and chitosan via self-assembly for delivery of anticancer drug, Colloids Surf. B Biointerfaces 146 (2016) 107-113, http://doi.org/10.1016/j.colsurfb.2016.05.043.
DOI Google Scholar
[49]

D. Wu, M. Wan, A novel fluoride anion modified gelatin nanogel system, J. Pharm. Pharm. Sci. 11 (2008) 32-45, http://doi.org/10.18433/J3988J.
DOI Google Scholar
[50]

Y. Serfert, C. Lamprecht, C.P. Tan, et al., Characterisation and use of β-lactoglobulin fibrils for microencapsulation of lipophilic ingredients and oxidative stability thereof, J. Food Eng. 143 (2014) 53-61, http://doi.org/10.1016/j.jfoodeng.2014.06.026.
DOI Google Scholar
[51]

M. Mohammadian, A. Madadlou, Technological functionality and biological properties of food protein nanofibrils formed by heating at acidic condition, Trends Food Sci. Technol. 75 (2018) 115-128, http://doi.org/10.1016/j.tifs.2018.03.013.
DOI Google Scholar
[52]

T. Farjami, A. Madadlou, M. Labbafi, Modulating the textural characteristics of whey protein nanofibril gels with different concentrations of calcium chloride, J. Dairy Res. 83 (2016) 109-114, http://doi.org/10.1017/S0022029915000667.
DOI Google Scholar
[53]

A. Kroes-Nijboer, P. Venema, E. van der Linden, Fibrillar structures in food, Food Funct. 3 (2012) 221-227, http://doi.org/10.1039/C1FO10163C.
DOI Google Scholar
[54]

S.G. Bolder, L.M. Sagis, P. Venema, et al., Effect of stirring and seeding on whey protein fibril formation, J. Agric. Food Chem. 55 (2007) 5661-5669, http://doi.org/10.1021/jf063351r.
DOI Google Scholar
[55]

C. Akkermans, P. Venema, A.J. van der Goot, et al., Peptides are building blocks of heat-induced fibrillar protein aggregates of β-lactoglobulin formed at pH 2, Biomacromolecules 9 (2008) 1474-1479, http://doi.org/10.1021/bm7014224.
DOI Google Scholar
[56]

M. Mohammadian, A. Madadlou, Characterization of fibrillated antioxidant whey protein hydrolysate and comparison with fibrillated protein solution, Food Hydrocoll. 52 (2016) 221-230, http://doi.org/10.1016/j.foodhyd.2015.06.022.
DOI Google Scholar
[57]

J. Adamcik, J.M. Jung, J. Flakowski, et al., Understanding amyloid aggregation by statistical analysis of atomic force microscopy images, Nat. Nanotechnol. 5 (2010) 423-428, http://doi.org/10.1038/nnano.2010.59.
DOI Google Scholar
[58]

M. Schleeger, T. Deckert-Gaudig, V. Deckert, et al., Amyloids: from molecular structure to mechanical properties, Polymer 54 (2013) 2473-2488, http://doi.org/10.1016/j.polymer.2013.02.029.
DOI Google Scholar
[59]

M. Mohammadian, M. Salami, S. Momen, et al., Enhancing the aqueous solubility of curcumin at acidic condition through the complexation with whey protein nanofibrils, Food Hydrocoll. 87 (2019) 902-914, http://doi.org/10.1016/j.foodhyd.2018.09.001.
DOI Google Scholar
[60]

M. Mohammadian, M. Salami, F. Alavi, et al., Fabrication and characterization of curcumin-loaded complex coacervates made of gum Arabic and whey protein nanofibrils, Food Biophys. 14 (2019) 425-436, http://doi.org/10.1007/s11483-019-09591-1.
DOI Google Scholar
[61]

Y. Shen, L. Posavec, S. Bolisetty, et al., Amyloid fibril systems reduce, stabilize and deliver bioavailable nanosized iron, Nat. Nanotechnol. 12 (2017) 642-651, http://doi.org/10.1038/nnano.2017.58.
DOI Google Scholar
[62]

S. Bolisetty, C.S. Boddupalli, S. Handschin, et al., Amyloid fibrils enhance transport of metal nanoparticles in living cells and induced cytotoxicity, Biomacromolecules 15 (2014) 2793-2799, http://doi.org/10.1021/bm500647n.
DOI Google Scholar
[63]

K.N.P. Humblet-Hua, G. Scheltens, E. van der Linden, et al., Encapsulation systems based on ovalbumin fibrils and high methoxyl pectin, Food Hydrocoll. 25 (2011) 307-314, http://doi.org/10.1016/j.foodhyd.2011.01.003.
DOI Google Scholar
[64]

E. Ansarifar, M. Mohebbi, F. Shahidi, et al., Novel multilayer microcapsules based on soy protein isolate fibrils and high methoxyl pectin: production, characterization and release modeling, Int. J. Biol. Macromol. 97 (2017) 761-769, http://doi.org/10.1016/j.ijbiomac.2017.01.056.
DOI Google Scholar
[65]

Y. Song, U. Shimanovich, T.C. Michaels, et al., Fabrication of fibrillosomes from droplets stabilized by protein nanofibrils at all-aqueous interfaces, Nature Comm. 7 (2016) 12934-12942, http://doi.org/10.1038/ncomms12934.
DOI Google Scholar
[66]

T. Farjami, A. Madadlou, M. Labbafi, Characteristics of the bulk hydrogels made of the citric acid cross-linked whey protein microgels, Food Hydrocoll. 50 (2015) 159-165, http://doi.org/10.1016/j.foodhyd.2015.04.011.
DOI Google Scholar
[67]

F. Alavi, S. Momen, Z. Emam-Djomeh, et al., Radical cross-linked whey protein aggregates as building blocks of non-heated cold-set gels, Food Hydrocoll. 81 (2018) 429-441, http://doi.org/10.1016/j.foodhyd.2018.03.016.
DOI Google Scholar
[68]

M. Mohammadian, M. Salami, Z. Emam-Djomeh, et al., Gelation of oil-in-water emulsions stabilized by heat-denatured and nanofibrillated whey proteins through ion bridging or citric acid-mediated cross-linking, Int. J. Biol. Macromol. 120 (2018) 2247-2258, http://doi.org/10.1016/j.ijbiomac.2018.08.085.
DOI Google Scholar
[69]

M. Mohammadian, A. Madadlou, Cold-set hydrogels made of whey protein nanofibrils with different divalent cations, Int. J. Biol. Macromol. 89 (2016) 499-506, http://doi.org/10.1016/j.ijbiomac.2016.05.009.
DOI Google Scholar
[70]

U. Shimanovich, I. Efimov, T.O. Mason, et al., Protein microgels from amyloid fibril networks, ACS Nano 9 (2015) 43-51, http://doi.org/10.1021/nn504869d.
DOI Google Scholar
[71]

S.T. Sullivan, C. Tang, A. Kennedy, et al., Electrospinning and heat treatment of whey protein nanofibers, Food Hydrocoll. 35 (2014) 36-50, http://doi.org/10.1016/j.foodhyd.2013.07.023.
DOI Google Scholar
[72]

W. Huang, T. Zou, S. Li, et al., Drug-loaded zein nanofibers prepared using a modified coaxial electrospinning process, AAPS Pharm. Sci. Tech. 14 (2013) 675-681, http://doi.org/10.1208/s12249-013-9953-1.
DOI Google Scholar
[73]

A.C. Mendes, K. Stephansen, I.S. Chronakis, Electrospinning of food proteins and polysaccharides, Food Hydrocoll. 68 (2017) 53-68, http://doi.org/10.1016/j.foodhyd.2016.10.022.
DOI Google Scholar
[74]

E. Tavassoli-Kafrani, S.A.H. Goli, M. Fathi, Encapsulation of orange essential oil using cross-linked electrospun gelatin nanofibers, Food Bioprocess. Technol. 11 (2018) 427-434, http://doi.org/10.1007/s11947-017-2026-9.
DOI Google Scholar
[75]

J. Zhong, S.D. Mohan, A. Bell, et al., Electrospinning of food-grade nanofibres from whey protein, Int. J. Biol. Macromol. 113 (2018) 764-773, http://doi.org/10.1016/j.ijbiomac.2018.02.113.
DOI Google Scholar
[76]

S. Wongsasulak, M. Patapeejumruswong, J. Weiss, et al., Electrospinning of food-grade nanofibers from cellulose acetate and egg albumen blends, J. Food Eng. 98 (2010) 370-376, http://doi.org/10.1016/j.jfoodeng.2010.01.014.
DOI Google Scholar
[77]

B. Ghorani, N. Tucker, Fundamentals of electrospinning as a novel delivery vehicle for bioactive compounds in food nanotechnology, Food Hydrocoll. 51 (2015) 227-240, http://doi.org/10.1016/j.foodhyd.2015.05.024.
DOI Google Scholar
[78]

H. Li, M. Wang, G.R. Williams, et al., Electrospun gelatin nanofibers loaded with vitamins A and E as antibacterial wound dressing materials, RSC Adv. 6 (2016) 50267-50277, http://doi.org/10.1039/C6RA05092A.
DOI Google Scholar
[79]

A. Fernandez, S. Torres-Giner, J.M. Lagaron, Novel route to stabilization of bioactive antioxidants by encapsulation in electrospun fibers of zein prolamine, Food Hydrocoll. 23 (2009) 1427-1432, http://doi.org/10.1016/j.foodhyd.2008.10.011.
DOI Google Scholar
[80]

H. Lu, Q. Wang, G. Li, et al., Electrospun water-stable zein/ethyl cellulose composite nanofiber and its drug release properties, Mater. Sci. Eng. C 74 (2017) 86-93, http://doi.org/10.1016/j.foodhyd.2008.10.011.
DOI Google Scholar
[81]

J.F. Graveland-Bikker, G. Fritz, O. Glatter, et al., Growth and structure of α-lactalbumin nanotubes, J. Appl. Cryst. 39 (2006) 180-184, http://doi.org/10.1107/S0021889805043244.
DOI Google Scholar
[82]

O. Tarhan, S. Harsa, Nanotubular structures developed from whey‐based α‐lactalbumin fractions for food applications, Biotechnol. Prog. 30 (2014) 1301-1310, http://doi.org/10.1002/btpr.1956.
DOI Google Scholar
[83]

D. Zhang, S.A. Dougherty, J. Liang, Fabrication of bovine serum albumin nanotubes through template-assisted layer by layer assembly, J. Nanopart. Res. 13 (2011) 1563-1571, http://doi.org/10.1002/btpr.1956.
DOI Google Scholar
[84]

R. Sadeghi, A. Kalbasi, Z. Emam-jomeh, et al., Biocompatible nanotubes as potential carrier for curcumin as a model bioactive compound, J. Nanopart. Res. 15 (2013) 1931-1942, http://doi.org/10.1007/s11051-013-1931-8.
DOI Google Scholar
[85]

I. Katouzian, S.M. Jafari, Protein nanotubes as state-of-the-art nanocarriers: synthesis methods, simulation and applications, J. Control. Release 303 (2019) 302-318, http://doi.org/10.1016/j.jconrel.2019.04.026.
DOI Google Scholar
[86]

X.L. Geng, M.J. Bjerrum, L. Arleth, et al., Formation of nanotubes and gels at a broad pH range upon partial hydrolysis of bovine α-lactalbumin, Int. Dairy J. 52 (2016) 72-81, http://doi.org/10.1016/j.colsurfb.2019.03.051.
DOI Google Scholar
[87]

J.F. Graveland-Bikker, C.G. de Kruif, Unique milk protein based nanotubes: food and nanotechnology meet, Trends Food Sci. Technol. 17 (2006) 196-203, http://doi.org/10.1016/j.tifs.2005.12.009.
DOI Google Scholar
[88]

P. Esmaeilzadeh, Z. Fakhroueian, P. Esmaeilzadeh, et al., Synthesis and characterization of various protein α-lactalbumin nanotubes structures by chemical hydrolysis method, Adv. Nanopart. 2 (2013) 154-164, http://doi.org/10.4236/anp.2013.22024.
DOI Google Scholar
[89]

J.F. Graveland-Bikker, R.I. Koning, H.K. Koerten, et al., Structural characterization of α-lactalbumin nanotubes, Soft Matter 5 (2009) 2020-2026, http://doi.org/10.1039/b815775h.
DOI Google Scholar
[90]

O. Tarhan, E. Tarhan, S. Harsa, Investigation of the structure of alpha-lactalbumin protein nanotubes using optical spectroscopy, J. Dairy Res. 81 (2014) 98-106, http://doi.org/10.1017/S0022029913000629.
DOI Google Scholar
[91]

C. Fuciños, M. Míguez, P. Fuciños, et al., Creating functional nanostructures: encapsulation of caffeine into α-lactalbumin nanotubes, Innov. Food Sci. Emergy Technol. 40 (2017) 10-17, http://doi.org/10.1016/j.ifset.2016.07.030.
DOI Google Scholar
[92]

L. Maldonado, J. Kokini, An optimal window for the fabrication of edible polyelectrolyte complex nanotubes (EPCNs) from bovine serum albumin (BSA) and sodium alginate, Food Hydrocoll. 77 (2017) 336-346, http://doi.org/10.1016/j.foodhyd.2017.10.010.
DOI Google Scholar
[93]

Y. Liu, Y. Cai, D. Ying, et al., Ovalbumin as a carrier to significantly enhance the aqueous solubility and photostability of curcumin: interaction and binding mechanism study, Int. J. Biol. Macromol. 116 (2018) 893-900, http://doi.org/10.1016/j.ijbiomac.2018.05.089.
DOI Google Scholar
[94]

E. Semo, E. Kesselman, D. Danino, et al., Casein micelle as a natural nano-capsular vehicle for nutraceuticals, Food Hydrocoll. 21 (2007) 936-942, http://doi.org/10.1016/j.foodhyd.2006.09.006.
DOI Google Scholar
[95]

A. Tapal, P.K. Tiku, Complexation of curcumin with soy protein isolate and its implications on solubility and stability of curcumin, Food Chem. 130 (2012) 960-965, http://doi.org/10.1016/j.foodchem.2011.08.025.
DOI Google Scholar
[96]

Y. Liu, D. Ying, Y. Cai, et al., Improved antioxidant activity and physicochemical properties of curcumin by adding ovalbumin and its structural characterization, Food Hydrocoll. 72 (2017) 304-311, http://doi.org/10.1016/j.foodhyd.2017.06.007.
DOI Google Scholar
[97]

F.P. Chen, B.S. Li, C.H. Tang, Nanocomplexation of soy protein isolate with curcumin: influence of ultrasonic treatment, Food Res. Int. 75 (2015) 157-165, http://doi.org/10.1016/j.foodres.2015.06.009.
DOI Google Scholar
[98]

Y. Liu, Y. Fan, L. Gao, et al., Enhanced pH and thermal stability, solubility and antioxidant activity of resveratrol by nanocomplexation with α-lactalbumin, Food Funct. 9 (2018) 4781-4790, http://doi.org/10.1039/C8FO01172A.
DOI Google Scholar
[99]

M. Esmaili, S.M. Ghaffari, Z. Moosavi-Movahedi, et al., Beta casein-micelle as a nano vehicle for solubility enhancement of curcumin; food industry application, LWT-Food Sci. Technol. 44 (2011) 2166-2172, http://doi.org/10.1016/j.lwt.2011.05.023.
DOI Google Scholar
[100]

D. Li, X. Li, G. Wu, et al., The characterization and stability of the soy protein isolate/1-octacosanol nanocomplex, Food Chem. 297 (2019) 124766, http://doi.org/10.1016/j.foodchem.2019.05.041.
DOI Google Scholar
[101]

F.F. Visentini, O.E. Sponton, A.A. Perez, et al., Formation and colloidal stability of ovalbumin-retinol nanocomplexes, Food Hydrocoll. 67 (2017) 130-138, http://doi.org/10.1016/j.foodhyd.2016.12.027.
DOI Google Scholar
[102]

A. Shpigelman, G. Israeli, Y.D. Livney, Thermally-induced protein–polyphenol co-assemblies: beta lactoglobulin-based nanocomplexes as protective nanovehicles for EGCG, Food Hydrocoll. 24 (2010) 735-743, http://doi.org/10.1016/j.foodhyd.2010.03.015.
DOI Google Scholar
[103]

Y. Wei, F. Vriesekoop, Q. Yuan, et al., β-Lactoglobulin as a nanotransporter for glabridin: exploring the binding properties and bioactivity influences, ACS Omega 3 (2018) 12246-12252, http://doi.org/10.1021/acsomega.8b01576.
DOI Google Scholar
[104]

F. Zhan, J. Hu, C. He, et al., Complexation between sodium caseinate and gallic acid: effects on foam properties and interfacial properties of foam, Food Hydrocoll. 99 (2020) 105365, http://doi.org/10.1016/j.foodhyd.2019.105365.
DOI Google Scholar
[105]

N. Pujara, S. Jambhrunkar, K.Y. Wong, et al., Enhanced colloidal stability, solubility and rapid dissolution of resveratrol by nanocomplexation with soy protein isolate, J. Colloid Interface Sci. 488 (2017) 303-308, http://doi.org/10.1016/j.jcis.2016.11.015.
DOI Google Scholar
[106]

S. Jiang, G. Yildiz, J. Ding, et al., Pea protein nanoemulsion and nanocomplex as carriers for protection of cholecalciferol (vitamin D3), Food Bioprocess Technol. 12 (2019) 1031-1040, http://doi.org/10.1007/s11947-019-02276-0.
DOI Google Scholar
[107]

N. Ghayour, S.M. Hosseini, M.H. Eskandari, et al., Nanoencapsulation of quercetin and curcumin in casein-based delivery systems, Food Hydrocoll. 87 (2019) 394-403, http://doi.org/10.1016/j.foodhyd.2018.08.031.
DOI Google Scholar
[108]

F. Rehan, N. Ahemad, M. Gupta, Casein nanomicelle as an emerging biomaterial–a comprehensive review, Colloids Surf. B Biointerfaces 179 (2019) 280-292, http://doi.org/10.1016/j.colsurfb.2019.03.051.
DOI Google Scholar
[109]

M.J. Sáiz-Abajo, C. González-Ferrero, A. Moreno-Ruiz, et al., Thermal protection of β-carotene in re-assembled casein micelles during different processing technologies applied in food industry, Food Chem. 138 (2013) 1581-1587, http://doi.org/10.1016/j.foodchem.2012.11.016.
DOI Google Scholar
[110]

P. Somu, S. Paul, Bio-conjugation of curcumin with self-assembled casein nanostructure via surface loading enhances its bioactivity: an efficient therapeutic system, Appl. Surf. Sci. 462 (2018) 316-329, http://doi.org/10.1016/j.apsusc.2018.08.094.
DOI Google Scholar
[111]

A. Loewen, B. Chan, E.C. Li-Chan, Optimization of vitamins A and D3 loading in re-assembled casein micelles and effect of loading on stability of vitamin D3 during storage, Food Chem. 240 (2018) 472-481, http://doi.org/10.1016/j.foodchem.2017.07.126.
DOI Google Scholar
[112]

Y. Cohen, M. Levi, U. Lesmes, et al., Re-assembled casein micelles improve in vitro bioavailability of vitamin D in a Caco-2 cell model, Food Funct. 8 (2017) 2133-2141, http://doi.org/10.1039/C7FO00323D.
DOI Google Scholar
[113]

P. Malekhosseini, M. Alami, M. Khomeiri, et al., Development of casein‐based nanoencapsulation systems for delivery of epigallocatechin gallate and folic acid, Food Sci. Nutr. 7 (2019) 519-527, http://doi.org/10.1002/fsn3.827.
DOI Google Scholar
[114]

K. Pan, Q. Zhong, S.J. Baek, Enhanced dispersibility and bioactivity of curcumin by encapsulation in casein nanocapsules, J. Agric. Food Chem. 61 (2013) 6036-6043, http://doi.org/10.1021/jf400752a.
DOI Google Scholar
[115]

K. Pan, Y. Luo, Y. Gan, et al., pH-driven encapsulation of curcumin in self-assembled casein nanoparticles for enhanced dispersibility and bioactivity, Soft Matter 10 (2014) 6820-6830, http://doi.org/10.1039/C4SM00239C.
DOI Google Scholar
[116]

Y. Zhang, S. He, Y. Ma, et al., Characterization and bioaccessibility of β-carotene in re-assembled casein, RSC Adv. 5 (2015) 77595-77600, http://doi.org/10.1039/C5RA07736B.
DOI Google Scholar
[117]

A. Rashidinejad, S.M. Loveday, G.B. Jameson, et al., Rutin-casein co-precipitates as potential delivery vehicles for flavonoid rutin, Food Hydrocoll. 96 (2019) 451-462, http://doi.org/10.1016/j.foodhyd.2019.05.032.
DOI Google Scholar
[118]

S. Gandhi, I. Roy, Doxorubicin-loaded casein nanoparticles for drug delivery: preparation, characterization and in vitro evaluation, Int. J. Biol. Macromol. 121 (2019) 6-12, http://doi.org/10.1016/j.ijbiomac.2018.10.005.
DOI Google Scholar
[119]

M. Bachar, A. Mandelbaum, I. Portnaya, et al., Development and characterization of a novel drug nanocarrier for oral delivery, based on self-assembled β-casein micelles, J. Control. Release 160 (2012) 164-171, http://doi.org/10.1016/j.jconrel.2012.01.004.
DOI Google Scholar
[120]

T.K. Głąb, J. Boratyński, Potential of casein as a carrier for biologically active agents, Top. Curr. Chem. 375 (2017) 71, http://doi.org/10.1007/s41061-017-0158-z.
DOI Google Scholar
[121]

L.L. Liu, X.T. Li, N. Zhang, et al., Novel soy β-conglycinin nanoparticles by ethanol-assisted disassembly and reassembly: outstanding nanocarriers for hydrophobic nutraceuticals, Food Hydrocoll. 91 (2019) 246-255, http://doi.org/10.1016/j.foodhyd.2019.01.042.
DOI Google Scholar
[122]

L.L. Liu, P.Z. Liu, X.T. Li, et al., Novel soy β-conglycinin core–shell nanoparticles as outstanding ecofriendly nanocarriers for curcumin, J. Agric. Food Chem. 67 (2019) 6292-6301, http://doi.org/10.1021/acs.jafc.8b05822.
DOI Google Scholar
[123]

E. Acosta, Bioavailability of nanoparticles in nutrient and nutraceutical delivery, Curr. Opin. Colloid Interface Sci. 14 (2009) 3-15, http://doi.org/10.1016/j.cocis.2008.01.002.
DOI Google Scholar
[124]

Y.D. Livney, Milk proteins as vehicles for bioactives, Curr. Opin. Colloid Interface Sci. 15 (2010) 73-83, http://doi.org/10.1016/j.cocis.2009.11.002.
DOI Google Scholar
[125]

P.N. Ezhilarasi, P. Karthik, N. Chhanwal, et al., Nanoencapsulation techniques for food bioactive components: a review, Food Bioprocess Technol. 6 (2013) 628-647, http://doi.org/10.1007/s11947-012-0944-0.
DOI Google Scholar
[126]

C.H. Tang, Nanostructured soy proteins: fabrication and applications as delivery systems for bioactives (a review), Food Hydrocoll. 91 (2019) 92-116, http://doi.org/10.1016/j.foodhyd.2019.01.012.
DOI Google Scholar
[127]

H. Li, D. Wang, C. Liu, et al., Fabrication of stable zein nanoparticles coated with soluble soybean polysaccharide for encapsulation of quercetin, Food Hydrocoll. 87 (2019) 342-351, http://doi.org/10.1016/j.foodhyd.2018.08.002.
DOI Google Scholar
[128]

D. Yang, Y. Li, J. Nie, Preparation of gelatin/PVA nanofibers and their potential application in controlled release of drugs, Carbohydr. Polym. 69 (2007) 538-543, http://doi.org/10.1016/j.carbpol.2007.01.008.
DOI Google Scholar
[129]

K. Karthikeyan, S. Guhathakarta, R. Rajaram, et al., Electrospun zein/eudragit nanofibers based dual drug delivery system for the simultaneous delivery of aceclofenac and pantoprazole, Int. J. Pharm. 438 (2012) 117-122, http://doi.org/10.1016/j.ijpharm.2012.07.075.
DOI Google Scholar
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Publication history

Received: 15 November 2019
Revised: 10 March 2020
Accepted: 10 April 2020
Published: 11 May 2020
Issue date: September 2020

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Acknowledgements

The support of University of Tehran and Iran National Science Foundation (INSF) is acknowledged.

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