메뉴 건너뛰기




Volumn 500, Issue 1-2, 2016, Pages 291-304

β-lactoglobulin stabilized nanemulsions - Formulation and process factors affecting droplet size and nanoemulsion stability

Author keywords

High pressure homogenization; Interfacial rheology; Interfacial tension; Nanoemulsions; Stability; Lactoglobulin

Indexed keywords

BETA LACTOGLOBULIN; MIGLYOL; OIL; WATER; EMULSION; LACTOGLOBULIN; NANOMATERIAL;

EID: 84957310480     PISSN: 03785173     EISSN: 18733476     Source Type: Journal    
DOI: 10.1016/j.ijpharm.2016.01.035     Document Type: Article
Times cited : (55)

References (106)
  • 1
    • 57049145802 scopus 로고    scopus 로고
    • Bioavailability of nanoparticles in nutrient and nutraceutical delivery
    • E. Acosta Bioavailability of nanoparticles in nutrient and nutraceutical delivery Curr. Opin. Colloid Interface Sci. 14 2009 3 15
    • (2009) Curr. Opin. Colloid Interface Sci. , vol.14 , pp. 3-15
    • Acosta, E.1
  • 2
    • 84899505722 scopus 로고    scopus 로고
    • Formation of whey protein isolate hydrolysate stabilised nanoemulsion
    • R. Adjonu, G. Doran, P. Torley, and S. Agboola Formation of whey protein isolate hydrolysate stabilised nanoemulsion Food Hydrocolloid 41 2014 169 177
    • (2014) Food Hydrocolloid , vol.41 , pp. 169-177
    • Adjonu, R.1    Doran, G.2    Torley, P.3    Agboola, S.4
  • 3
    • 84855715840 scopus 로고    scopus 로고
    • Nanoemulsion- and emulsion-based delivery systems for curcumin: Encapsulation and release properties
    • K. Ahmed, Y. Li, D.J. McClements, and H. Xiao Nanoemulsion- and emulsion-based delivery systems for curcumin: encapsulation and release properties Food Chem. 132 2012 799 807
    • (2012) Food Chem. , vol.132 , pp. 799-807
    • Ahmed, K.1    Li, Y.2    McClements, D.J.3    Xiao, H.4
  • 4
    • 84970926858 scopus 로고    scopus 로고
    • Can protein functionalities be enhanced by high-pressure homogenization? - A study on functional properties of lupin Proteins
    • S. Bader, J. Bez, and P. Eisner Can protein functionalities be enhanced by high-pressure homogenization? - A study on functional properties of lupin Proteins Procedia Food Sci. 1 2011 1359 1366
    • (2011) Procedia Food Sci. , vol.1 , pp. 1359-1366
    • Bader, S.1    Bez, J.2    Eisner, P.3
  • 5
    • 84928638837 scopus 로고    scopus 로고
    • Effect of high pressure-low temperature treatments on structural characteristics of whey proteins and micellar caseins
    • D. Baier, B. Purschke, C. Schmitt, H.M. Rawel, and D. Knorr Effect of high pressure-low temperature treatments on structural characteristics of whey proteins and micellar caseins Food Chem. 187 2015 354 363
    • (2015) Food Chem. , vol.187 , pp. 354-363
    • Baier, D.1    Purschke, B.2    Schmitt, C.3    Rawel, H.M.4    Knorr, D.5
  • 6
    • 33746577383 scopus 로고    scopus 로고
    • Compression/expansion rheology of oil/water interfaces with adsorbed proteins: Comparison with the air/water surface
    • J. Benjamins, J. Lyklema, and E.H. Lucassen-Reynders Compression/expansion rheology of oil/water interfaces with adsorbed proteins: comparison with the air/water surface Langmuir 22 2006 6181 6188
    • (2006) Langmuir , vol.22 , pp. 6181-6188
    • Benjamins, J.1    Lyklema, J.2    Lucassen-Reynders, E.H.3
  • 7
    • 84874375346 scopus 로고    scopus 로고
    • Intracellular fate of retinyl acetate-loaded submicron delivery systems by in vitro intestinal epithelial cells: A comparison between whey protein-stabilised submicron droplets and micelles stabilised with polysorbate 80
    • A. Benzaria, D. Chevalier-Lucia, L. Picart-Palmade, P. Hue, T. López-Pedemonte, and E. Dumay Intracellular fate of retinyl acetate-loaded submicron delivery systems by in vitro intestinal epithelial cells: a comparison between whey protein-stabilised submicron droplets and micelles stabilised with polysorbate 80 Food Res. Int. 51 2013 679 692
    • (2013) Food Res. Int. , vol.51 , pp. 679-692
    • Benzaria, A.1    Chevalier-Lucia, D.2    Picart-Palmade, L.3    Hue, P.4    López-Pedemonte, T.5    Dumay, E.6
  • 8
    • 0032798799 scopus 로고    scopus 로고
    • Protein adsorption at the oil/water interface: Characterization of adsorption kinetics by dynamic interfacial tension measurements
    • C.J. Beverung, C.J. Radke, and H.W. Blanch Protein adsorption at the oil/water interface: characterization of adsorption kinetics by dynamic interfacial tension measurements Biophys. Chem. 81 1999 59 80
    • (1999) Biophys. Chem. , vol.81 , pp. 59-80
    • Beverung, C.J.1    Radke, C.J.2    Blanch, H.W.3
  • 9
    • 30344478568 scopus 로고    scopus 로고
    • Functional properties of whey proteins as affected by dynamic high-pressure treatment
    • H. Bouaouina, A. Desrumaux, C. Loisel, and J. Legrand Functional properties of whey proteins as affected by dynamic high-pressure treatment Int. Dairy J. 16 2006 275 284
    • (2006) Int. Dairy J. , vol.16 , pp. 275-284
    • Bouaouina, H.1    Desrumaux, A.2    Loisel, C.3    Legrand, J.4
  • 10
    • 84878441283 scopus 로고    scopus 로고
    • β-Lactoglobulin, gum Arabic, and xanthan gum for emulsifying sweet almond oil: Formulation and stabilization mechanisms of pharmaceutical emulsions
    • E. Bouyer, G. Mekhloufi, N. Huang, V. Rosilio, and F. Agnely β-Lactoglobulin, gum arabic, and xanthan gum for emulsifying sweet almond oil: formulation and stabilization mechanisms of pharmaceutical emulsions Colloid Surf. A 433 2013 77 87
    • (2013) Colloid Surf. A , vol.433 , pp. 77-87
    • Bouyer, E.1    Mekhloufi, G.2    Huang, N.3    Rosilio, V.4    Agnely, F.5
  • 12
    • 84865281543 scopus 로고    scopus 로고
    • Proteins, polysaccharides, and their complexes used as stabilizers for emulsions: Alternatives to synthetic surfactants in the pharmaceutical field?
    • E. Bouyer, G. Mekhloufi, V. Rosilio, J.-L. Grossiord, and F. Agnely Proteins, polysaccharides, and their complexes used as stabilizers for emulsions: alternatives to synthetic surfactants in the pharmaceutical field? Int. J. Pharm. 436 2012 359 378
    • (2012) Int. J. Pharm. , vol.436 , pp. 359-378
    • Bouyer, E.1    Mekhloufi, G.2    Rosilio, V.3    Grossiord, J.-L.4    Agnely, F.5
  • 14
    • 79953685905 scopus 로고    scopus 로고
    • Nanonization strategies for poorly water-soluble drugs
    • H. Chen, C. Khemtong, X. Yang, X. Chang, and J. Gao Nanonization strategies for poorly water-soluble drugs Drug Discov. Today 16 7-8 2011 354 360
    • (2011) Drug Discov. Today , vol.16 , Issue.7-8 , pp. 354-360
    • Chen, H.1    Khemtong, C.2    Yang, X.3    Chang, X.4    Gao, J.5
  • 15
    • 34548033224 scopus 로고    scopus 로고
    • Preparation and characterization of beta-carotene nanodispersions prepared by solvent displacement technique
    • B.S. Chu, S. Ichikawa, S. Kanafusa, and M. Nakajima Preparation and characterization of beta-carotene nanodispersions prepared by solvent displacement technique J. Agric. Food Chem. 55 2007 6754 6760
    • (2007) J. Agric. Food Chem. , vol.55 , pp. 6754-6760
    • Chu, B.S.1    Ichikawa, S.2    Kanafusa, S.3    Nakajima, M.4
  • 16
    • 54249165361 scopus 로고    scopus 로고
    • Characteristics of submicron emulsions prepared by ultra-high pressure homogenisation: Effect of chilled or frozen storage
    • M. Cortés-Muňoz, D. Chevalier-Lucia, and E. Dumay Characteristics of submicron emulsions prepared by ultra-high pressure homogenisation: effect of chilled or frozen storage Food Hydrocolloid 23 2009 640 654
    • (2009) Food Hydrocolloid , vol.23 , pp. 640-654
    • Cortés-Muňoz, M.1    Chevalier-Lucia, D.2    Dumay, E.3
  • 17
    • 0038157337 scopus 로고    scopus 로고
    • Formation of sunflower oil emulsions stabilized by whey proteins with high-pressure homogenization (up to 350 MPa): Wffect of pressure on emulsion characteristics
    • A. Desrumaux, and J. Marcand Formation of sunflower oil emulsions stabilized by whey proteins with high-pressure homogenization (up to 350 MPa): wffect of pressure on emulsion characteristics Int. Journal Food Sci. Technol. 37 2002 263 269
    • (2002) Int. Journal Food Sci. Technol. , vol.37 , pp. 263-269
    • Desrumaux, A.1    Marcand, J.2
  • 19
    • 0026026073 scopus 로고
    • Time-dependent polymerization of β-lactoglobulin through disulphide bonds at the oil-water interface in emulsions
    • E. Dickinson, and Y. Matsumura Time-dependent polymerization of β-lactoglobulin through disulphide bonds at the oil-water interface in emulsions Int. J. Biol Macromol. 13 1 1991 26 30
    • (1991) Int. J. Biol Macromol. , vol.13 , Issue.1 , pp. 26-30
    • Dickinson, E.1    Matsumura, Y.2
  • 20
    • 0000298096 scopus 로고    scopus 로고
    • Properties of emulsions stabilized with milk proteins: Overview of some recent developments
    • E. Dickinson Properties of emulsions stabilized with milk proteins: overview of some recent developments J. Dairy Sci. 80 1997 2607 2619
    • (1997) J. Dairy Sci. , vol.80 , pp. 2607-2619
    • Dickinson, E.1
  • 22
    • 78049291493 scopus 로고    scopus 로고
    • Development of novel pea protein-based nanoemulsions for delivery of nutraceuticals
    • F. Donsì, B. Senatore, Q. Huang, and G. Ferrari Development of novel pea protein-based nanoemulsions for delivery of nutraceuticals J. Agric. Food Chem. 58 2010 10653 10660
    • (2010) J. Agric. Food Chem. , vol.58 , pp. 10653-10660
    • Donsì, F.1    Senatore, B.2    Huang, Q.3    Ferrari, G.4
  • 24
    • 0023283514 scopus 로고
    • Binding of p-nitrophenol phosphate and other aromatic-compounds to β-lactoglobulin
    • H.M. Farrell, M.J. Behe, and J.A. Enyeart Binding of p-nitrophenol phosphate and other aromatic-compounds to β-lactoglobulin J. Dairy Sci. 70 2 1987 252 258
    • (1987) J. Dairy Sci. , vol.70 , Issue.2 , pp. 252-258
    • Farrell, H.M.1    Behe, M.J.2    Enyeart, J.A.3
  • 25
    • 1642324504 scopus 로고    scopus 로고
    • Analysis of a new type of high pressure homogeniser: A study of the flow pattern
    • J. Floury, J. Bellettre, J. Legrand, and A. Desrumaux Analysis of a new type of high pressure homogeniser: a study of the flow pattern Chem. Eng. Sci. 59 2004 843 853
    • (2004) Chem. Eng. Sci. , vol.59 , pp. 843-853
    • Floury, J.1    Bellettre, J.2    Legrand, J.3    Desrumaux, A.4
  • 26
    • 0034196519 scopus 로고    scopus 로고
    • Effect of high-pressure homogenization on droplet sizedistributions and rheological properties of model oil-in-water emulsions
    • J. Floury, A. Desrumaux, and J. Lardieres Effect of high-pressure homogenization on droplet sizedistributions and rheological properties of model oil-in-water emulsions Innov. Food Sci. Emerg. Technol. 1 2000 127 134
    • (2000) Innov. Food Sci. Emerg. Technol. , vol.1 , pp. 127-134
    • Floury, J.1    Desrumaux, A.2    Lardieres, J.3
  • 27
    • 0015443657 scopus 로고
    • Scanning isoelectric focusing in small density gradient columns II: Microfractionation of column contents. Evaluation of pH course. Isoelectric points of β-lactoglobulins A and B
    • S. Fredriksson Scanning isoelectric focusing in small density gradient columns II: microfractionation of column contents. Evaluation of pH course. Isoelectric points of β-lactoglobulins A and B Anal. Biochem. 50 1972 575 585
    • (1972) Anal. Biochem. , vol.50 , pp. 575-585
    • Fredriksson, S.1
  • 29
    • 84894094426 scopus 로고    scopus 로고
    • Effects of unsaturation and different ring-opening methods on the properties of vegetable oil-based polyurethane coatings
    • T.F. Garrison, M.R. Kessler, and R.C. Larock Effects of unsaturation and different ring-opening methods on the properties of vegetable oil-based polyurethane coatings Polymer 55 2014 1004 1011
    • (2014) Polymer , vol.55 , pp. 1004-1011
    • Garrison, T.F.1    Kessler, M.R.2    Larock, R.C.3
  • 30
    • 0034880214 scopus 로고    scopus 로고
    • Cremophor EL: The drawbacks and advantages of vehicle selection for drug formulation
    • H. Gelderblom, J. Verweij, K. Nooter, and A. Sparreboom Cremophor EL: the drawbacks and advantages of vehicle selection for drug formulation Eur. J. Cancer 37 2001 1590 1598
    • (2001) Eur. J. Cancer , vol.37 , pp. 1590-1598
    • Gelderblom, H.1    Verweij, J.2    Nooter, K.3    Sparreboom, A.4
  • 31
    • 0019927017 scopus 로고
    • Dispersion phenomena in high viscosity immiscible fluid systems and application of static mixers as dispersion devices in such systems
    • H.P. Grace Dispersion phenomena in high viscosity immiscible fluid systems and application of static mixers as dispersion devices in such systems Chem. Eng. Commun. 14 1982 225
    • (1982) Chem. Eng. Commun. , vol.14 , pp. 225
    • Grace, H.P.1
  • 32
    • 33947425055 scopus 로고    scopus 로고
    • Impact of electrostatic interactions on formation and stability of emulsions containing oil droplets coated by β-lactoglobulin-pectin complexes
    • D. Guzey, and D.J. McClements Impact of electrostatic interactions on formation and stability of emulsions containing oil droplets coated by β-lactoglobulin-pectin complexes J. Agric. Food Chem. 55 2 2007 475 485
    • (2007) J. Agric. Food Chem. , vol.55 , Issue.2 , pp. 475-485
    • Guzey, D.1    McClements, D.J.2
  • 33
    • 42649132499 scopus 로고    scopus 로고
    • Protein nanoparticles as drug carriers in clinical medicine
    • M.J. Hawkins, P. Soon-Shiong, and N. Desai Protein nanoparticles as drug carriers in clinical medicine Adv. Drug Deliv. Rev. 60 2008 876 885
    • (2008) Adv. Drug Deliv. Rev. , vol.60 , pp. 876-885
    • Hawkins, M.J.1    Soon-Shiong, P.2    Desai, N.3
  • 34
    • 0001118101 scopus 로고
    • Utilization of pressure in addition to temperature in food science and technology
    • C. Balny, R. Hayashi, K. Heremans, P. Masson, Colloque INSERM/John Libbey Eurotext Ltd.
    • R. Hayashi Utilization of pressure in addition to temperature in food science and technology C. Balny, R. Hayashi, K. Heremans, P. Masson, High Pressure and Biotechnology vol. 224 1992 Colloque INSERM/John Libbey Eurotext Ltd. 185 193
    • (1992) High Pressure and Biotechnology , vol.224 , pp. 185-193
    • Hayashi, R.1
  • 35
    • 84874153505 scopus 로고    scopus 로고
    • Nanoemulsion-templated shell-crosslinked nanocapsules as drug delivery systems
    • W. He, Y. Lu, J. Qi, L. Chen, F. Hu, and W. Wu Nanoemulsion-templated shell-crosslinked nanocapsules as drug delivery systems Int. J. Pharm. 445 2013 69 78
    • (2013) Int. J. Pharm. , vol.445 , pp. 69-78
    • He, W.1    Lu, Y.2    Qi, J.3    Chen, L.4    Hu, F.5    Wu, W.6
  • 36
    • 80053329082 scopus 로고    scopus 로고
    • Food protein-stabilized nanoemulsions as potential delivery systems for poorly water-soluble drugs: Preparation, in vitro characterization, and pharmacokinetics in rats
    • W. He, Y. Tan, Z. Tian, L. Chen, F. Hu, and W. Wu Food protein-stabilized nanoemulsions as potential delivery systems for poorly water-soluble drugs: preparation, in vitro characterization, and pharmacokinetics in rats Int. J. Nanomed. 6 2011 521 533
    • (2011) Int. J. Nanomed. , vol.6 , pp. 521-533
    • He, W.1    Tan, Y.2    Tian, Z.3    Chen, L.4    Hu, F.5    Wu, W.6
  • 37
    • 0038309868 scopus 로고    scopus 로고
    • Physico-chemical stability of colloidal lipid particles. Physico-chemical stability of colloidal lipid particles
    • B. Heurtault, P. Saulnier, B. Pech, J.-E. Proust, and J.-P. Benoit Physico-chemical stability of colloidal lipid particles. Physico-chemical stability of colloidal lipid particles Biomaterials 24 23 2003 4283 4300
    • (2003) Biomaterials , vol.24 , Issue.23 , pp. 4283-4300
    • Heurtault, B.1    Saulnier, P.2    Pech, B.3    Proust, J.-E.4    Benoit, J.-P.5
  • 38
    • 0037860910 scopus 로고    scopus 로고
    • A model for large deformation of an ellipsoidal droplet with interfacial tension
    • N.E. Jackson, and C.L. Tucker A model for large deformation of an ellipsoidal droplet with interfacial tension J. Rheol. 47 2003 659 682
    • (2003) J. Rheol. , vol.47 , pp. 659-682
    • Jackson, N.E.1    Tucker, C.L.2
  • 39
    • 44349155539 scopus 로고    scopus 로고
    • Re-coalescence of emulsion droplets during high-energy emulsification
    • S.M. Jafari, E. Assadpoor, Y. He, and B. Bhandari Re-coalescence of emulsion droplets during high-energy emulsification Food Hydrocolloid 22 2008 1191 1202
    • (2008) Food Hydrocolloid , vol.22 , pp. 1191-1202
    • Jafari, S.M.1    Assadpoor, E.2    He, Y.3    Bhandari, B.4
  • 40
    • 34250637454 scopus 로고    scopus 로고
    • Optimization of nano-emulsions production by microfluidization
    • S.M. Jafari, Y. He, and B. Bhandari Optimization of nano-emulsions production by microfluidization Eur. Food Res. Technol. 225 2007 733 741
    • (2007) Eur. Food Res. Technol. , vol.225 , pp. 733-741
    • Jafari, S.M.1    He, Y.2    Bhandari, B.3
  • 41
    • 2442635332 scopus 로고    scopus 로고
    • A Recombinant C121S mutant of bovine β-Lactoglobulin is more susceptible to peptic digestion and to denaturation by reducing agents and heating
    • D. Jayat, J.C. Gaudin, J.M. Chobert, T.V. Burova, C. Holt, I. McNae, L. Sawyer, and T. Haertlé A Recombinant C121S mutant of bovine β-Lactoglobulin is more susceptible to peptic digestion and to denaturation by reducing agents and heating Biochemistry 43 2004 6312 6321
    • (2004) Biochemistry , vol.43 , pp. 6312-6321
    • Jayat, D.1    Gaudin, J.C.2    Chobert, J.M.3    Burova, T.V.4    Holt, C.5    McNae, I.6    Sawyer, L.7    Haertlé, T.8
  • 42
    • 10044272158 scopus 로고    scopus 로고
    • Influence of free protein on flocculation stability of β-Lactoglobulin stabilized oil-in-water emulsions at neutral pH and ambient temperature
    • H.-J. Kim, E.A. Decker, and D.J. McClements Influence of free protein on flocculation stability of β-Lactoglobulin stabilized oil-in-water emulsions at neutral pH and ambient temperature Langmuir 20 2004 10394 10398
    • (2004) Langmuir , vol.20 , pp. 10394-10398
    • Kim, H.-J.1    Decker, E.A.2    McClements, D.J.3
  • 43
    • 0036812540 scopus 로고    scopus 로고
    • Role of postadsorption conformation changes of β-lactoglobulin on its ability to stabilize oil droplets against flocculation during heating at neutral
    • H.J. Kim, E.A. Decker, and D.J. McClements Role of postadsorption conformation changes of β-lactoglobulin on its ability to stabilize oil droplets against flocculation during heating at neutral Langmuir 18 2002 7577 7583
    • (2002) Langmuir , vol.18 , pp. 7577-7583
    • Kim, H.J.1    Decker, E.A.2    McClements, D.J.3
  • 44
    • 0042161817 scopus 로고    scopus 로고
    • Protein adsorption at liquid/liquid interface with low interfacial tension
    • È. Kiss, and R. Borbás Protein adsorption at liquid/liquid interface with low interfacial tension Colloid Surf. B 31 2003 169 176
    • (2003) Colloid Surf. B , vol.31 , pp. 169-176
    • Kiss, È.1    Borbás, R.2
  • 45
    • 0035281869 scopus 로고    scopus 로고
    • Evaluation of a new high-pressure dispersion unit (HPN) for emulsification
    • G. Kolb, K. Viardot, G. Wagner, and J. Ulrich Evaluation of a new high-pressure dispersion unit (HPN) for emulsification Chem. Eng. Technol. 24 2001 293 296
    • (2001) Chem. Eng. Technol. , vol.24 , pp. 293-296
    • Kolb, G.1    Viardot, K.2    Wagner, G.3    Ulrich, J.4
  • 46
    • 4243120936 scopus 로고    scopus 로고
    • Invited Review: β-lactoglobulin: Binding properties, structure, and function
    • G. Kontopidis, C. Holt, and L. Sawyer Invited Review: β-lactoglobulin: binding properties, structure, and function J. Dairy Sci. 87 4 2004 785 796
    • (2004) J. Dairy Sci. , vol.87 , Issue.4 , pp. 785-796
    • Kontopidis, G.1    Holt, C.2    Sawyer, L.3
  • 47
    • 84859947948 scopus 로고    scopus 로고
    • Exploring oral nanoemulsionsfor bioavailability enhancement of poorly water-soluble drugs
    • S. Kotta, A.W. Khan, K. Pramod, S.H. Ansari, R.K. Sharma, and J. Ali Exploring oral nanoemulsionsfor bioavailability enhancement of poorly water-soluble drugs Expert Opin. Drug Deliv. 9 5 2012 585 598
    • (2012) Expert Opin. Drug Deliv. , vol.9 , Issue.5 , pp. 585-598
    • Kotta, S.1    Khan, A.W.2    Pramod, K.3    Ansari, S.H.4    Sharma, R.K.5    Ali, J.6
  • 48
    • 84878310546 scopus 로고    scopus 로고
    • Food proteins: A review on their emulsifying properties using a structure-function approach
    • R.S.H. Lam, and M.T. Nickerson Food proteins: a review on their emulsifying properties using a structure-function approach Food Chem. 141 2013 975 984
    • (2013) Food Chem. , vol.141 , pp. 975-984
    • Lam, R.S.H.1    Nickerson, M.T.2
  • 51
    • 78651064318 scopus 로고    scopus 로고
    • Protein-stabilized nanoemulsions and emulsions: Comparison of physicochemical stability, lipid oxidation, and lipase digestibility
    • S.J. Lee, S.J. Choi, Y. Li, E.A. Decker, and D.J. McClements Protein-stabilized nanoemulsions and emulsions: Comparison of physicochemical stability, lipid oxidation, and lipase digestibility J. Agric. Food Chem. 59 2011 415 427
    • (2011) J. Agric. Food Chem. , vol.59 , pp. 415-427
    • Lee, S.J.1    Choi, S.J.2    Li, Y.3    Decker, E.A.4    McClements, D.J.5
  • 52
    • 53149142432 scopus 로고    scopus 로고
    • Effects of ultra-high pressure homogenization on the properties and structure of interfacial protein layer in whey protein-stabilized emulsion
    • S.H. Lee, T. Lefèvre, M. Subirade, and P. Paquin Effects of ultra-high pressure homogenization on the properties and structure of interfacial protein layer in whey protein-stabilized emulsion Food Chem. 113 2009 191 195
    • (2009) Food Chem. , vol.113 , pp. 191-195
    • Lee, S.H.1    Lefèvre, T.2    Subirade, M.3    Paquin, P.4
  • 53
    • 77955090797 scopus 로고    scopus 로고
    • Fabrication of protein-stabilized nanoemulsions using a combined homogenization and amphiphilic solvent dissolution/evaporation approach
    • S.J. Lee, and D.J. McClements Fabrication of protein-stabilized nanoemulsions using a combined homogenization and amphiphilic solvent dissolution/evaporation approach Food Hydrocolloid 24 2010 560 569
    • (2010) Food Hydrocolloid , vol.24 , pp. 560-569
    • Lee, S.J.1    McClements, D.J.2
  • 54
    • 0038172338 scopus 로고    scopus 로고
    • Formation of intermolecular β-sheet structures: A phenomenon relevant to protein film structure at oil-water interfaces of emulsions
    • T. Lefèvre, and M. Subirade Formation of intermolecular β-sheet structures: a phenomenon relevant to protein film structure at oil-water interfaces of emulsions J. Colloid Interface Sci. 263 2003 59 67
    • (2003) J. Colloid Interface Sci. , vol.263 , pp. 59-67
    • Lefèvre, T.1    Subirade, M.2
  • 56
    • 84903752995 scopus 로고    scopus 로고
    • Whey-protein-stabilized nanoemulsions as a potential delivery system for water-insoluble curcumin
    • M. Li, Y. Ma, and J. Cui Whey-protein-stabilized nanoemulsions as a potential delivery system for water-insoluble curcumin LWT-Food Sci. Technol. 59 2014 49 58
    • (2014) LWT-Food Sci. Technol. , vol.59 , pp. 49-58
    • Li, M.1    Ma, Y.2    Cui, J.3
  • 57
    • 84864749488 scopus 로고    scopus 로고
    • Physical and antimicrobial properties of peppermint oil nanoemulsions
    • R. Liang, S. Xu, C.F. Shoemaker, Y. Li, F. Zhong, and Q. Huang Physical and antimicrobial properties of peppermint oil nanoemulsions Agric. Food Chem. 60 2012 7548 7555
    • (2012) Agric. Food Chem. , vol.60 , pp. 7548-7555
    • Liang, R.1    Xu, S.2    Shoemaker, C.F.3    Li, Y.4    Zhong, F.5    Huang, Q.6
  • 60
    • 84871508634 scopus 로고    scopus 로고
    • Preparation and application of nanoemulsions in the last decade (2000-2010)
    • A. Maali, and M.T.H. Mosavian Preparation and application of nanoemulsions in the last decade (2000-2010) J. Dispersion Sci. Technol. 34 2013 92 105
    • (2013) J. Dispersion Sci. Technol. , vol.34 , pp. 92-105
    • Maali, A.1    Mosavian, M.T.H.2
  • 61
    • 0037338158 scopus 로고    scopus 로고
    • Monodisperse fragmentation in emulsions: Mechanisms and kinetics
    • C. Mabille, F. Leal-Calderon, J. Bibette, and V. Schmitt Monodisperse fragmentation in emulsions: mechanisms and kinetics Europhys. Lett. 61 2003 708 714
    • (2003) Europhys. Lett. , vol.61 , pp. 708-714
    • Mabille, C.1    Leal-Calderon, F.2    Bibette, J.3    Schmitt, V.4
  • 62
    • 80054727280 scopus 로고    scopus 로고
    • Optimization of β-casein stabilized nanoemulsions using experimental mixture design
    • P.G. Maher, M.A. Fenelon, Y. Zhou, M.K. Haque, and Y.H. Roos Optimization of β-casein stabilized nanoemulsions using experimental mixture design J. Food Sci. 76 8 2011 C1108 17
    • (2011) J. Food Sci. , vol.76 , Issue.8 , pp. C1108-C1117
    • Maher, P.G.1    Fenelon, M.A.2    Zhou, Y.3    Haque, M.K.4    Roos, Y.H.5
  • 63
    • 70349387891 scopus 로고    scopus 로고
    • Effects of small and large molecule emulsifiers on the characteristics of beta-carotene nanoemulsions prepared by high pressure homogenization
    • L. Mao, D. Xu, J. Yang, F. Yuan, Y. Gao, and J. Zhao Effects of small and large molecule emulsifiers on the characteristics of beta-carotene nanoemulsions prepared by high pressure homogenization Food Technol. Biotechnol. 47 3 2009 336 342
    • (2009) Food Technol. Biotechnol. , vol.47 , Issue.3 , pp. 336-342
    • Mao, L.1    Xu, D.2    Yang, J.3    Yuan, F.4    Gao, Y.5    Zhao, J.6
  • 66
    • 0004130627 scopus 로고    scopus 로고
    • Food emulsions: Principles, practice, and techniques
    • 2nd ed. CRC Press Boca Raton
    • D.J. McClements Food emulsions: Principles, practice, and techniques CRC Series in Contemporary Food Science 2nd ed. 2005 CRC Press Boca Raton
    • (2005) CRC Series in Contemporary Food Science
    • McClements, D.J.1
  • 67
    • 79952390166 scopus 로고    scopus 로고
    • Edible nanoemulsions: Fabrication, properties, and functional performance
    • D.J. McClements Edible nanoemulsions: fabrication, properties, and functional performance Soft Matter 7 2011 2297 2316
    • (2011) Soft Matter , vol.7 , pp. 2297-2316
    • McClements, D.J.1
  • 68
    • 22944476741 scopus 로고    scopus 로고
    • Surface dilational rheology of mixed beta-lactoglobulin/surfactant layers at the air/water interface
    • R. Miller, M.E. Leser, M. Michel, and V.B. Fainerman Surface dilational rheology of mixed beta-lactoglobulin/surfactant layers at the air/water interface J. Phys. Chem. B 109 27 2005 13327 13331
    • (2005) J. Phys. Chem. B , vol.109 , Issue.27 , pp. 13327-13331
    • Miller, R.1    Leser, M.E.2    Michel, M.3    Fainerman, V.B.4
  • 69
    • 0031214433 scopus 로고    scopus 로고
    • Coalescence of protein-stabilized emulsions in a high-pressure homogenizer
    • S. Mohan, and G. Narsimhan Coalescence of protein-stabilized emulsions in a high-pressure homogenizer J. Colloid Interface Sci. 192 1997 1 15
    • (1997) J. Colloid Interface Sci. , vol.192 , pp. 1-15
    • Mohan, S.1    Narsimhan, G.2
  • 70
    • 79952532291 scopus 로고    scopus 로고
    • Exploitation of maize germ for the preparation of a stable oil-body nanoemulsion using a combined aqueous extraction ultrafiltration method
    • C.V. Nikiforidis, O.A. Karkani, and V. Kiosseoglou Exploitation of maize germ for the preparation of a stable oil-body nanoemulsion using a combined aqueous extraction ultrafiltration method Food Hydrocolloid 25 2011 1122 1127
    • (2011) Food Hydrocolloid , vol.25 , pp. 1122-1127
    • Nikiforidis, C.V.1    Karkani, O.A.2    Kiosseoglou, V.3
  • 71
    • 6944228179 scopus 로고    scopus 로고
    • Effect of pressure and fat content on particle sizes in microfluidized milk
    • D.W. Olson, C.H. White, and R.L. Richter Effect of pressure and fat content on particle sizes in microfluidized milk J. Dairy Sci. 87 2004 3217 3223
    • (2004) J. Dairy Sci. , vol.87 , pp. 3217-3223
    • Olson, D.W.1    White, C.H.2    Richter, R.L.3
  • 72
    • 0032840936 scopus 로고    scopus 로고
    • Technological properties of high pressure homogenizers: The effect of fat globules, milk proteins, and polysaccharides
    • P. Paquin Technological properties of high pressure homogenizers: the effect of fat globules, milk proteins, and polysaccharides Int. Dairy J. 9 1999 329 335
    • (1999) Int. Dairy J. , vol.9 , pp. 329-335
    • Paquin, P.1
  • 73
    • 0029302371 scopus 로고
    • Interaction of β-lactoglobulin with retinol and fatty acids and its role as a possible biological function for this protein A review
    • M.D. Pérez, and M. Calvo Interaction of β-lactoglobulin with retinol and fatty acids and its role as a possible biological function for this protein A review J. Dairy Sci. 78 5 1995 978 988
    • (1995) J. Dairy Sci. , vol.78 , Issue.5 , pp. 978-988
    • Pérez, M.D.1    Calvo, M.2
  • 74
    • 84865202089 scopus 로고    scopus 로고
    • Nanoemulsions for drug delivery through different routes
    • R.T.U. Prakash, and P. Thiagarajan Nanoemulsions for drug delivery through different routes Res. Biotechnol. 2 3 2011 01 13
    • (2011) Res. Biotechnol. , vol.2 , Issue.3 , pp. 01-13
    • Prakash, R.T.U.1    Thiagarajan, P.2
  • 75
    • 84856212477 scopus 로고    scopus 로고
    • Physical and chemical stability of beta-carotene-enriched nanoemulsions: Influence of pH, ionic strength, temperature, and emulsifier type
    • C. Qian, E.A. Decker, H. Xiao, and D.J. McClements Physical and chemical stability of beta-carotene-enriched nanoemulsions: influence of pH, ionic strength, temperature, and emulsifier type Food Chem. 132 2012 1221 1229
    • (2012) Food Chem. , vol.132 , pp. 1221-1229
    • Qian, C.1    Decker, E.A.2    Xiao, H.3    McClements, D.J.4
  • 76
    • 79952534865 scopus 로고    scopus 로고
    • Formation of nanoemulsions stabilized by model food-grade emulsifiers using high-pressure homogenization: Factors affecting particle size
    • C. Qian, and D.J. McClements Formation of nanoemulsions stabilized by model food-grade emulsifiers using high-pressure homogenization: factors affecting particle size Food Hydrocolloid 25 2011 1000 1008
    • (2011) Food Hydrocolloid , vol.25 , pp. 1000-1008
    • Qian, C.1    McClements, D.J.2
  • 77
    • 70350757645 scopus 로고    scopus 로고
    • Factors affecting vitamin degradation in oil-in-water nano-emulsions
    • P. Relkin, J.M. Jung, and M. Ollivon Factors affecting vitamin degradation in oil-in-water nano-emulsions J. Therm. Anal. Calorim. 98 2009 13 18
    • (2009) J. Therm. Anal. Calorim. , vol.98 , pp. 13-18
    • Relkin, P.1    Jung, J.M.2    Ollivon, M.3
  • 78
    • 78049314185 scopus 로고    scopus 로고
    • Encapsulation of epigallocatechin-3-gallate (EGCG) using oil-in-water (O/W) submicrometer emulsions stabilized by τ-carrageenan and β-lactoglobulin
    • Q. Ru, H. Yu, and Q. Huang Encapsulation of epigallocatechin-3-gallate (EGCG) using oil-in-water (O/W) submicrometer emulsions stabilized by τ-carrageenan and β-lactoglobulin J. Agric. Food Chem. 58 2010 10373 10381
    • (2010) J. Agric. Food Chem. , vol.58 , pp. 10373-10381
    • Ru, Q.1    Yu, H.2    Huang, Q.3
  • 79
    • 55549125193 scopus 로고    scopus 로고
    • Adsorption and structural change of β-Lactoglobulin at the diacylglycerol-water interface
    • M.M. Sakuno, S. Matsumoto, S. Kawai, K. Taihei, and Y. Matsumura Adsorption and structural change of β-Lactoglobulin at the diacylglycerol-water interface Langmuir 24 2008 11483 11488
    • (2008) Langmuir , vol.24 , pp. 11483-11488
    • Sakuno, M.M.1    Matsumoto, S.2    Kawai, S.3    Taihei, K.4    Matsumura, Y.5
  • 82
    • 0034684161 scopus 로고    scopus 로고
    • The core lipocalin, bovine β-lactoglobulin
    • L. Sawyer, and G. Kontopidis The core lipocalin, bovine β-lactoglobulin Biochim. Biophys. Acta 1482 2000 136 148
    • (2000) Biochim. Biophys. Acta , vol.1482 , pp. 136-148
    • Sawyer, L.1    Kontopidis, G.2
  • 83
    • 30444440706 scopus 로고    scopus 로고
    • Formation and charaterization of submicrometer oil-in-water (O/W) emulsions using high-energy emulsification
    • I.N. Seekkuarachchi, K. Tanaka, and H. Kumazawa Formation and charaterization of submicrometer oil-in-water (O/W) emulsions using high-energy emulsification Ind. Eng. Chem. Res. 45 2006 372 390
    • (2006) Ind. Eng. Chem. Res. , vol.45 , pp. 372-390
    • Seekkuarachchi, I.N.1    Tanaka, K.2    Kumazawa, H.3
  • 84
    • 84887547108 scopus 로고    scopus 로고
    • Rheology and adsorption behaviour of β-casein and β-lactoglobulin mixed layers at the sunflower oil/water interface
    • L. Seta, N. Baldino, D. Gabriele, F.R. Lupi, and B.D. Cindio Rheology and adsorption behaviour of β-casein and β-lactoglobulin mixed layers at the sunflower oil/water interface Colloid Surf. A 441 2014 669 677
    • (2014) Colloid Surf. A , vol.441 , pp. 669-677
    • Seta, L.1    Baldino, N.2    Gabriele, D.3    Lupi, F.R.4    Cindio, B.D.5
  • 85
    • 79952491335 scopus 로고    scopus 로고
    • Nanoemulsions: A pharmaceutical review
    • P. Shah, D. Bhalodia, and P. Shelat Nanoemulsions: a pharmaceutical review Syst. Rev. Pharm. 1 1 2010 24 32
    • (2010) Syst. Rev. Pharm. , vol.1 , Issue.1 , pp. 24-32
    • Shah, P.1    Bhalodia, D.2    Shelat, P.3
  • 88
    • 0014770081 scopus 로고
    • Binding of long chain fatty acids to β-lactoglobulin
    • A.A. Spector, and J.E. Fletcher Binding of long chain fatty acids to β-lactoglobulin Lipids 5 4 1970 403 411
    • (1970) Lipids , vol.5 , Issue.4 , pp. 403-411
    • Spector, A.A.1    Fletcher, J.E.2
  • 89
    • 0032001694 scopus 로고    scopus 로고
    • Effect of dynamic high pressure on the secondary structure of β-Lactoglobulin and on its conformational properties as determined by Fourier Transform Infrared Spectroscopy
    • M. Subirade, F. Loupil, A.F. Allain, and P. Paquin Effect of dynamic high pressure on the secondary structure of β-Lactoglobulin and on its conformational properties as determined by Fourier Transform Infrared Spectroscopy Int. Dairy J. 8 1998 135 140
    • (1998) Int. Dairy J. , vol.8 , pp. 135-140
    • Subirade, M.1    Loupil, F.2    Allain, A.F.3    Paquin, P.4
  • 92
    • 70349230769 scopus 로고    scopus 로고
    • Formulation of multifunctional oil-in-water nanosized emulsions for active and passive targeting of drugs to otherwise inaccessible internal organs of the human body
    • S. Tamilvanan Formulation of multifunctional oil-in-water nanosized emulsions for active and passive targeting of drugs to otherwise inaccessible internal organs of the human body Int. J. Pharm. 381 2009 62 76
    • (2009) Int. J. Pharm. , vol.381 , pp. 62-76
    • Tamilvanan, S.1
  • 93
    • 0000180414 scopus 로고
    • The formation of emulsions in definable fields of flow
    • G.I. Taylor The formation of emulsions in definable fields of flow Proc. R. Soc. A146 1934 501
    • (1934) Proc. R. Soc. , vol.146 A , pp. 501
    • Taylor, G.I.1
  • 94
    • 4444222206 scopus 로고    scopus 로고
    • Role of surfactant type and concentration for the mean drop size during emulsification in turbulent flow
    • S. Tcholakova, N.D. Denkov, and T. Danner Role of surfactant type and concentration for the mean drop size during emulsification in turbulent flow Langmuir 20 2004 7444 7458
    • (2004) Langmuir , vol.20 , pp. 7444-7458
    • Tcholakova, S.1    Denkov, N.D.2    Danner, T.3
  • 95
    • 0037069481 scopus 로고    scopus 로고
    • Coalescence in β-lactoglobulin-stabilized emulsions: Effects of protein adsorption and drop size
    • S. Tcholakova, N.D. Denkov, I.B. Ivanov, and B. Campbell Coalescence in β-lactoglobulin-stabilized emulsions: Effects of protein adsorption and drop size Langmuir 18 2002 8960 8971
    • (2002) Langmuir , vol.18 , pp. 8960-8971
    • Tcholakova, S.1    Denkov, N.D.2    Ivanov, I.B.3    Campbell, B.4
  • 96
    • 0000819131 scopus 로고
    • Molecular interactions in β-lactoglobulin. II. Ultracentrifugal and electrophoretic studies of the association of β-lactoglobulin below its isoelectric point
    • R. Townend, R.J. Winterbottom, and S.N. Timasheff Molecular interactions in β-lactoglobulin. II. Ultracentrifugal and electrophoretic studies of the association of β-lactoglobulin below its isoelectric point J. Am. Chem. Soc. 82 12 1960 3161 3168
    • (1960) J. Am. Chem. Soc. , vol.82 , Issue.12 , pp. 3161-3168
    • Townend, R.1    Winterbottom, R.J.2    Timasheff, S.N.3
  • 97
    • 0026791626 scopus 로고
    • Principles of emulsion formation
    • P. Walstra Principles of emulsion formation Chem. Eng. Sci. 48 2 1993 333 349
    • (1993) Chem. Eng. Sci. , vol.48 , Issue.2 , pp. 333-349
    • Walstra, P.1
  • 99
    • 79960157053 scopus 로고    scopus 로고
    • Impact of free fatty acid concentration and structure on lipid oxidation in oil-in-water emulsions
    • T. Waraho, D.J. McClements, and E.A. Decker Impact of free fatty acid concentration and structure on lipid oxidation in oil-in-water emulsions Food Chem. 129 2011 854 859
    • (2011) Food Chem. , vol.129 , pp. 854-859
    • Waraho, T.1    McClements, D.J.2    Decker, E.A.3
  • 100
    • 57349166030 scopus 로고    scopus 로고
    • Impact of oil type on nanoemulsion formation and Ostwald ripening stability
    • T.J. Wooster, M. Golding, and P. Sanguansri Impact of oil type on nanoemulsion formation and Ostwald ripening stability Langmuir 24 2008 12758 12765
    • (2008) Langmuir , vol.24 , pp. 12758-12765
    • Wooster, T.J.1    Golding, M.2    Sanguansri, P.3
  • 101
    • 0141617182 scopus 로고    scopus 로고
    • Interfacial dilational behaviour of adsorbed β-lactoglobulin layers at the different fluid interfaces
    • R. Wüstneck, B. Moser, and G. Muschiolik Interfacial dilational behaviour of adsorbed β-lactoglobulin layers at the different fluid interfaces Colloid Surf. B: Biointerfaces 15 1999 263 273
    • (1999) Colloid Surf. B: Biointerfaces , vol.15 , pp. 263-273
    • Wüstneck, R.1    Moser, B.2    Muschiolik, G.3
  • 102
    • 84862840686 scopus 로고    scopus 로고
    • Stable nano-sized emulsions produced from soy protein and soy polysaccharide complexes
    • B. Yin, W. Deng, K. Xu, L. Huang, and P. Yao Stable nano-sized emulsions produced from soy protein and soy polysaccharide complexes J. Colloid Interface Sci. 380 2012 51 59
    • (2012) J. Colloid Interface Sci. , vol.380 , pp. 51-59
    • Yin, B.1    Deng, W.2    Xu, K.3    Huang, L.4    Yao, P.5
  • 103
    • 84856035282 scopus 로고    scopus 로고
    • Effects of limited enzymatic hydrolysis with pepsin and high-pressure homogenization on the functional properties of soybean protein isolate
    • B. Yuan, J. Ren, M. Zhao, D. Luo, and L. Gu Effects of limited enzymatic hydrolysis with pepsin and high-pressure homogenization on the functional properties of soybean protein isolate LWT-Food Sci. Technol. 46 2012 453 459
    • (2012) LWT-Food Sci. Technol. , vol.46 , pp. 453-459
    • Yuan, B.1    Ren, J.2    Zhao, M.3    Luo, D.4    Gu, L.5
  • 104
    • 84906055604 scopus 로고    scopus 로고
    • Impact of alcohols on the formation and stability of protein-stabilized NEs
    • B. Zeeb, E. Herz, D.J. McClements, and J. Weiss Impact of alcohols on the formation and stability of protein-stabilized NEs J. Colloid Interface Sci. 433 2014 196 203
    • (2014) J. Colloid Interface Sci. , vol.433 , pp. 196-203
    • Zeeb, B.1    Herz, E.2    McClements, D.J.3    Weiss, J.4
  • 105
    • 79960770032 scopus 로고    scopus 로고
    • Structural rearrangement of β-Lactoglobulin at different oil-water interfaces and its effect on emulsion stability
    • J. Zhai, T.J. Wooster, S.V. Hoffmann, T.H. Lee, M.A. Augustin, and M.I. Aguilar Structural rearrangement of β-Lactoglobulin at different oil-water interfaces and its effect on emulsion stability Langmuir 27 2011 9227 9236
    • (2011) Langmuir , vol.27 , pp. 9227-9236
    • Zhai, J.1    Wooster, T.J.2    Hoffmann, S.V.3    Lee, T.H.4    Augustin, M.A.5    Aguilar, M.I.6
  • 106
    • 84864053225 scopus 로고    scopus 로고
    • Aggregation and conformational changes of bovine β-lactoglobulin subjected to dynamic high-pressure microfluidization in relation to antigenicity
    • J.Z. Zhong, W. Liu, C.M. Liu, Q.H. Wang, T. Li, Z.C. Tu, S.J. Luo, X.F. Cai, and Y.J. Xu Aggregation and conformational changes of bovine β-lactoglobulin subjected to dynamic high-pressure microfluidization in relation to antigenicity J. Dairy Sci. 95 2012 4237 4245
    • (2012) J. Dairy Sci. , vol.95 , pp. 4237-4245
    • Zhong, J.Z.1    Liu, W.2    Liu, C.M.3    Wang, Q.H.4    Li, T.5    Tu, Z.C.6    Luo, S.J.7    Cai, X.F.8    Xu, Y.J.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.