메뉴 건너뛰기




Volumn 5, Issue 44, 2015, Pages 35138-35154

Beta-lactoglobulin-based encapsulating systems as emerging bioavailability enhancers for nutraceuticals: A review

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; BIODEGRADABLE POLYMERS; BIODEGRADATION; PROTEINS;

EID: 84928320966     PISSN: None     EISSN: 20462069     Source Type: Journal    
DOI: 10.1039/c5ra01814e     Document Type: Review
Times cited : (91)

References (113)
  • 1
    • 33646008554 scopus 로고    scopus 로고
    • Food protein-based materials as nutraceutical delivery systems
    • L. Chen G. E. Remondetto M. Subirade Food protein-based materials as nutraceutical delivery systems Trends Food Sci. Technol. 2006 17 272 283
    • (2006) Trends Food Sci. Technol. , vol.17 , pp. 272-283
    • Chen, L.1    Remondetto, G.E.2    Subirade, M.3
  • 3
    • 84885848402 scopus 로고    scopus 로고
    • Overview of Microencapsulates for Use in Food Products or Processes and Methods to Make Them
    • in, ed. N. J. Zuidam and V. Nedovic, Springer New York
    • N. Zuidam and E. Shimoni, Overview of Microencapsulates for Use in Food Products or Processes and Methods to Make Them, in Encapsulation Technologies for Active Food Ingredients and Food Processing, ed., N. J. Zuidam, and, V. Nedovic, Springer New York, 2010, pp. 3-29
    • (2010) Encapsulation Technologies for Active Food Ingredients and Food Processing , pp. 3-29
    • Zuidam, N.1    Shimoni, E.2
  • 6
    • 0033992170 scopus 로고    scopus 로고
    • Desolvation process and surface characterisation of protein nanoparticles
    • C. Weber C. Coester J. Kreuter K. Langer Desolvation process and surface characterisation of protein nanoparticles Int. J. Pharm. 2000 194 91 102
    • (2000) Int. J. Pharm. , vol.194 , pp. 91-102
    • Weber, C.1    Coester, C.2    Kreuter, J.3    Langer, K.4
  • 9
    • 84881253553 scopus 로고    scopus 로고
    • Cationic β-Lactoglobulin Nanoparticles as a Bioavailability Enhancer: Protein Characterization and Particle Formation
    • Z. Teng Y. Li Y. Luo B. Zhang Q. Wang Cationic β-Lactoglobulin Nanoparticles as a Bioavailability Enhancer: Protein Characterization and Particle Formation Biomacromolecules 2013 14 2848 2856
    • (2013) Biomacromolecules , vol.14 , pp. 2848-2856
    • Teng, Z.1    Li, Y.2    Luo, Y.3    Zhang, B.4    Wang, Q.5
  • 10
    • 34247880387 scopus 로고    scopus 로고
    • Effect of β-Lactoglobulin A and B Whey Protein Variants on the Rennet-Induced Gelation of Skim Milk Gels in a Model Reconstituted Skim Milk System
    • M. A. Meza-Nieto B. Vallejo-Cordoba A. F. González-Córdova L. Félix F. M. Goycoolea Effect of β-Lactoglobulin A and B Whey Protein Variants on the Rennet-Induced Gelation of Skim Milk Gels in a Model Reconstituted Skim Milk System J. Dairy Sci. 2007 90 582 593
    • (2007) J. Dairy Sci. , vol.90 , pp. 582-593
    • Meza-Nieto, M.A.1    Vallejo-Cordoba, B.2    González-Córdova, A.F.3    Félix, L.4    Goycoolea, F.M.5
  • 11
    • 0034769732 scopus 로고    scopus 로고
    • Salt-dependent monomer-dimer equilibrium of bovine beta-lactoglobulin at pH 3
    • K. Sakurai M. Oobatake Y. Goto Salt-dependent monomer-dimer equilibrium of bovine beta-lactoglobulin at pH 3 Protein Sci. 2001 10 2325 2335
    • (2001) Protein Sci. , vol.10 , pp. 2325-2335
    • Sakurai, K.1    Oobatake, M.2    Goto, Y.3
  • 12
    • 70149121260 scopus 로고    scopus 로고
    • Electrostatic effects on β-lactoglobulin transitions during heat denaturation as studied by differential scanning calorimetry
    • I. J. Haug H. M. Skar G. E. Vegarud T. Langsrud K. I. Draget Electrostatic effects on β-lactoglobulin transitions during heat denaturation as studied by differential scanning calorimetry Food Hydrocolloids 2009 23 2287 2293
    • (2009) Food Hydrocolloids , vol.23 , pp. 2287-2293
    • Haug, I.J.1    Skar, H.M.2    Vegarud, G.E.3    Langsrud, T.4    Draget, K.I.5
  • 13
    • 84928350264 scopus 로고    scopus 로고
    • Comparative Analysis of Chemical and Thermal Denatured β-Lactoglobulin AB in the Presence of Casein
    • Z. Saadati and A. Razzaghi, Comparative Analysis of Chemical and Thermal Denatured β-Lactoglobulin AB in the Presence of Casein, Advanced Studies in Biology, 2012, 4, 255 264, http://www.m-hikari.com/asb/
    • (2012) Advanced Studies in Biology , vol.4 , pp. 255-264
    • Saadati, Z.1    Razzaghi, A.2
  • 14
    • 0036037132 scopus 로고    scopus 로고
    • The ligand-binding site of bovine β-lactoglobulin: Evidence for a function?
    • G. Kontopidis C. Holt L. Sawyer The ligand-binding site of bovine β-lactoglobulin: evidence for a function? J. Mol. Biol. 2002 318 1043 1055
    • (2002) J. Mol. Biol. , vol.318 , pp. 1043-1055
    • Kontopidis, G.1    Holt, C.2    Sawyer, L.3
  • 15
    • 0028246854 scopus 로고
    • Probing the retinol-binding site of bovine beta-lactoglobulin
    • Y. Cho C. A. Batt L. Sawyer Probing the retinol-binding site of bovine beta-lactoglobulin J. Biol. Chem. 1994 269 11102 11107
    • (1994) J. Biol. Chem. , vol.269 , pp. 11102-11107
    • Cho, Y.1    Batt, C.A.2    Sawyer, L.3
  • 16
    • 4243120936 scopus 로고    scopus 로고
    • Invited Review: β-Lactoglobulin: Binding Properties, Structure, and Function
    • G. Kontopidis C. Holt L. Sawyer Invited Review: β-Lactoglobulin: Binding Properties, Structure, and Function J. Dairy Sci. 2004 87 785 796
    • (2004) J. Dairy Sci. , vol.87 , pp. 785-796
    • Kontopidis, G.1    Holt, C.2    Sawyer, L.3
  • 17
    • 0031892161 scopus 로고    scopus 로고
    • Mapping fatty acid binding to β-lactoglobulin: Ligand binding is restricted by modification of Cys 121
    • M. Narayan L. J. Berliner Mapping fatty acid binding to β-lactoglobulin: Ligand binding is restricted by modification of Cys 121 Protein Sci. 1998 7 150 157
    • (1998) Protein Sci. , vol.7 , pp. 150-157
    • Narayan, M.1    Berliner, L.J.2
  • 19
    • 0031160714 scopus 로고    scopus 로고
    • Binding of Vitamin D and Cholesterol to β-Lactoglobulin
    • Q. Wang J. C. Allen H. E. Swaisgood Binding of Vitamin D and Cholesterol to β-Lactoglobulin J. Dairy Sci. 1997 80 1054 1059
    • (1997) J. Dairy Sci. , vol.80 , pp. 1054-1059
    • Wang, Q.1    Allen, J.C.2    Swaisgood, H.E.3
  • 20
    • 0034633086 scopus 로고    scopus 로고
    • Bioactive peptides derived from bovine whey proteins: Opioid and ace-inhibitory peptides
    • A. Pihlanto-Leppälä Bioactive peptides derived from bovine whey proteins: opioid and ace-inhibitory peptides Trends Food Sci. Technol. 2000 11 347 356
    • (2000) Trends Food Sci. Technol. , vol.11 , pp. 347-356
    • Pihlanto-Leppälä, A.1
  • 22
    • 84896939359 scopus 로고    scopus 로고
    • Tangeretin-loaded protein nanoparticles fabricated from zein/β-lactoglobulin: Preparation, characterization, and functional performance
    • J. Chen J. Zheng D. J. McClements H. Xiao Tangeretin-loaded protein nanoparticles fabricated from zein/β-lactoglobulin: Preparation, characterization, and functional performance Food Chem. 2014 158 466 472
    • (2014) Food Chem. , vol.158 , pp. 466-472
    • Chen, J.1    Zheng, J.2    McClements, D.J.3    Xiao, H.4
  • 23
    • 0000443256 scopus 로고
    • Structural and Conformational Basis of the Resistance of Beta-Lactoglobulin to Peptic and Chymotryptic Digestion
    • I. M. Reddy N. K. D. Kella J. E. Kinsella Structural and Conformational Basis of the Resistance of Beta-Lactoglobulin to Peptic and Chymotryptic Digestion J. Agric. Food Chem. 1988 36 737 741
    • (1988) J. Agric. Food Chem. , vol.36 , pp. 737-741
    • Reddy, I.M.1    Kella, N.K.D.2    Kinsella, J.E.3
  • 24
    • 58649115800 scopus 로고    scopus 로고
    • Protein nanoparticle: A unique system as drug delivery vehicles
    • M. Jahanshahi Z. Babaei Protein nanoparticle: A unique system as drug delivery vehicles Afr. J. Biotechnol. 2008 7 4926 4934
    • (2008) Afr. J. Biotechnol. , vol.7 , pp. 4926-4934
    • Jahanshahi, M.1    Babaei, Z.2
  • 25
    • 0035937590 scopus 로고    scopus 로고
    • Nanoparticulate systems for improved drug delivery
    • Y. Kawashima Nanoparticulate systems for improved drug delivery Adv. Drug Delivery Rev. 2001 47 1 2
    • (2001) Adv. Drug Delivery Rev. , vol.47 , pp. 1-2
    • Kawashima, Y.1
  • 26
    • 0003377551 scopus 로고
    • Lipid encapsulation technology-techniques and applications to food
    • R. Matsuno S. Adachi Lipid encapsulation technology-techniques and applications to food Trends Food Sci. Technol. 1993 4 256 261
    • (1993) Trends Food Sci. Technol. , vol.4 , pp. 256-261
    • Matsuno, R.1    Adachi, S.2
  • 28
    • 84863011608 scopus 로고    scopus 로고
    • Development of zein nanoparticles coated with carboxymethyl chitosan for encapsulation and controlled release of vitamin D3
    • Y. Luo Z. Teng Q. Wang Development of zein nanoparticles coated with carboxymethyl chitosan for encapsulation and controlled release of vitamin D3 J. Agric. Food Chem. 2012 60 836 843
    • (2012) J. Agric. Food Chem. , vol.60 , pp. 836-843
    • Luo, Y.1    Teng, Z.2    Wang, Q.3
  • 29
    • 79955652517 scopus 로고    scopus 로고
    • Preparation and characterization of zein/chitosan complex for encapsulation of α-tocopherol, and its in vitro controlled release study
    • Y. Luo B. Zhang M. Whent L. L. Yu Q. Wang Preparation and characterization of zein/chitosan complex for encapsulation of α-tocopherol, and its in vitro controlled release study Colloids Surf., B 2011 85 145 152
    • (2011) Colloids Surf., B , vol.85 , pp. 145-152
    • Luo, Y.1    Zhang, B.2    Whent, M.3    Yu, L.L.4    Wang, Q.5
  • 30
    • 84863011608 scopus 로고    scopus 로고
    • Development of zein nanoparticles coated with carboxymethyl chitosan for encapsulation and controlled release of vitamin D3
    • Y. Luo Z. Teng Q. Wang Development of zein nanoparticles coated with carboxymethyl chitosan for encapsulation and controlled release of vitamin D3 J. Agric. Food Chem. 2012 836 843
    • (2012) J. Agric. Food Chem. , pp. 836-843
    • Luo, Y.1    Teng, Z.2    Wang, Q.3
  • 31
    • 33745001604 scopus 로고    scopus 로고
    • Mucin structure, aggregation, physiological functions and biomedical applications
    • R. Bansil B. S. Turner Mucin structure, aggregation, physiological functions and biomedical applications Curr. Opin. Colloid Interface Sci. 2006 11 164 170
    • (2006) Curr. Opin. Colloid Interface Sci. , vol.11 , pp. 164-170
    • Bansil, R.1    Turner, B.S.2
  • 32
    • 40849136145 scopus 로고    scopus 로고
    • Evaluation of mucoadhesiveness of polymers by BIACORE method and mucin-particle method
    • J. Thongborisute H. Takeuchi Evaluation of mucoadhesiveness of polymers by BIACORE method and mucin-particle method Int. J. Pharm. 2008 354 204 209
    • (2008) Int. J. Pharm. , vol.354 , pp. 204-209
    • Thongborisute, J.1    Takeuchi, H.2
  • 33
    • 0026865864 scopus 로고
    • PH-dependent interactions between adsorbed chitosan layers
    • P. M. Claesson B. W. Ninham pH-dependent interactions between adsorbed chitosan layers Langmuir 1992 8 1406 1412
    • (1992) Langmuir , vol.8 , pp. 1406-1412
    • Claesson, P.M.1    Ninham, B.W.2
  • 34
    • 0036451610 scopus 로고    scopus 로고
    • Chitosan and sodium alginate-based bioadhesive vaginal tablets
    • A. El-Kamel M. Sokar V. Naggar S. Al Gamal Chitosan and sodium alginate-based bioadhesive vaginal tablets AAPS PharmSci 2002 4 224 230
    • (2002) AAPS PharmSci , vol.4 , pp. 224-230
    • El-Kamel, A.1    Sokar, M.2    Naggar, V.3    Al Gamal, S.4
  • 37
    • 0033035543 scopus 로고    scopus 로고
    • Renal drug delivery with low-molecular-weight proteins: The effect of charge modifications on the body distribution of drug-lysozyme conjugates
    • R. J. Kok F. Grijpstra K. H. Nederhoed F. Moolenaar Renal drug delivery with low-molecular-weight proteins: The effect of charge modifications on the body distribution of drug-lysozyme conjugates Drug Delivery 1999 6 1 8
    • (1999) Drug Delivery , vol.6 , pp. 1-8
    • Kok, R.J.1    Grijpstra, F.2    Nederhoed, K.H.3    Moolenaar, F.4
  • 39
    • 36848999897 scopus 로고    scopus 로고
    • Cell Penetrating Peptide-Coated Nanoribbons for Intracellular Nanocarriers
    • Y.-B. Lim E. Lee M. Lee Cell Penetrating Peptide-Coated Nanoribbons for Intracellular Nanocarriers Angew. Chem. 2007 119 3545 3548
    • (2007) Angew. Chem. , vol.119 , pp. 3545-3548
    • Lim, Y.-B.1    Lee, E.2    Lee, M.3
  • 41
    • 0343882023 scopus 로고    scopus 로고
    • Targeted drug delivery via the folate receptor
    • J. Sudimack R. J. Lee Targeted drug delivery via the folate receptor Adv. Drug Delivery Rev. 2000 41 147 162
    • (2000) Adv. Drug Delivery Rev. , vol.41 , pp. 147-162
    • Sudimack, J.1    Lee, R.J.2
  • 42
    • 38849129380 scopus 로고    scopus 로고
    • Interaction of β-Lactoglobulin with Resveratrol and its Biological Implications
    • L. Liang H. A. Tajmir-Riahi M. Subirade Interaction of β-Lactoglobulin with Resveratrol and its Biological Implications Biomacromolecules 2007 9 50 56
    • (2007) Biomacromolecules , vol.9 , pp. 50-56
    • Liang, L.1    Tajmir-Riahi, H.A.2    Subirade, M.3
  • 43
    • 78049267292 scopus 로고    scopus 로고
    • Interaction of Curcumin with β-Lactoglobulin-Stability, Spectroscopic Analysis, and Molecular Modeling of the Complex
    • A. H. Sneharani J. V. Karakkat S. A. Singh A. G. A. Rao Interaction of Curcumin with β-Lactoglobulin-Stability, Spectroscopic Analysis, and Molecular Modeling of the Complex J. Agric. Food Chem. 2010 58 11130 11139
    • (2010) J. Agric. Food Chem. , vol.58 , pp. 11130-11139
    • Sneharani, A.H.1    Karakkat, J.V.2    Singh, S.A.3    Rao, A.G.A.4
  • 44
    • 77955052598 scopus 로고    scopus 로고
    • Thermally-induced protein-polyphenol co-assemblies: Beta lactoglobulin-based nanocomplexes as protective nanovehicles for EGCG
    • A. Shpigelman G. Israeli Y. D. Livney Thermally-induced protein-polyphenol co-assemblies: beta lactoglobulin-based nanocomplexes as protective nanovehicles for EGCG Food Hydrocolloids 2010 24 735 743
    • (2010) Food Hydrocolloids , vol.24 , pp. 735-743
    • Shpigelman, A.1    Israeli, G.2    Livney, Y.D.3
  • 45
    • 84866395406 scopus 로고    scopus 로고
    • β-Lactoglobulin as a Molecular Carrier of Linoleate: Characterization and Effects on Intestinal Epithelial Cells in Vitro
    • S. L. Maux L. Giblin T. Croguennec S. Bouhallab A. Brodkorb β-Lactoglobulin as a Molecular Carrier of Linoleate: Characterization and Effects on Intestinal Epithelial Cells in Vitro J. Agric. Food Chem. 2012 60 9476 9483
    • (2012) J. Agric. Food Chem. , vol.60 , pp. 9476-9483
    • Maux, S.L.1    Giblin, L.2    Croguennec, T.3    Bouhallab, S.4    Brodkorb, A.5
  • 46
    • 84878226466 scopus 로고    scopus 로고
    • Protective effect of ligand-binding proteins against folic acid loss due to photodecomposition
    • L. Liang J. Zhang P. Zhou M. Subirade Protective effect of ligand-binding proteins against folic acid loss due to photodecomposition Food Chem. 2013 141 754 761
    • (2013) Food Chem. , vol.141 , pp. 754-761
    • Liang, L.1    Zhang, J.2    Zhou, P.3    Subirade, M.4
  • 47
    • 77952531665 scopus 로고    scopus 로고
    • β-Lactoglobulin/folic acid complexes: Formation, characterization, and biological implication
    • L. Liang M. Subirade β-Lactoglobulin/folic acid complexes: formation, characterization, and biological implication J. Phys. Chem. B 2010 114 6707 6712
    • (2010) J. Phys. Chem. B , vol.114 , pp. 6707-6712
    • Liang, L.1    Subirade, M.2
  • 48
    • 57749091590 scopus 로고    scopus 로고
    • Beta-lactoglobulin and its nanocomplexes with pectin as vehicles for ω-3 polyunsaturated fatty acids
    • P. Zimet Y. D. Livney Beta-lactoglobulin and its nanocomplexes with pectin as vehicles for ω-3 polyunsaturated fatty acids Food Hydrocolloids 2009 23 1120 1126
    • (2009) Food Hydrocolloids , vol.23 , pp. 1120-1126
    • Zimet, P.1    Livney, Y.D.2
  • 49
    • 84879244104 scopus 로고    scopus 로고
    • Complexes between linoleate and native or aggregated β-lactoglobulin: Interaction parameters and in vitro cytotoxic effect
    • S. L. Maux S. Bouhallab L. Giblin A. Brodkorb T. Croguennec Complexes between linoleate and native or aggregated β-lactoglobulin: Interaction parameters and in vitro cytotoxic effect Food Chem. 2013 141 2305 2313
    • (2013) Food Chem. , vol.141 , pp. 2305-2313
    • Maux, S.L.1    Bouhallab, S.2    Giblin, L.3    Brodkorb, A.4    Croguennec, T.5
  • 50
    • 84906860992 scopus 로고    scopus 로고
    • Insight into Curcumin-Loaded β-Lactoglobulin Nanoparticles: Incorporation, Particle Disintegration, and Releasing Profiles
    • Z. Teng Y. Li Q. Wang Insight into Curcumin-Loaded β-Lactoglobulin Nanoparticles: Incorporation, Particle Disintegration, and Releasing Profiles J. Agric. Food Chem. 2014 62 8837 8847
    • (2014) J. Agric. Food Chem. , vol.62 , pp. 8837-8847
    • Teng, Z.1    Li, Y.2    Wang, Q.3
  • 51
    • 84901653530 scopus 로고    scopus 로고
    • Fabrication of Coated Bovine Serum Albumin (BSA)-Epigallocatechin gallate (EGCG) Nanoparticles and Their Transport across Monolayers of Human Intestinal Epithelial Caco-2 Cells
    • Z. Li J.-H. Ha T. Zou L. Gu Fabrication of Coated Bovine Serum Albumin (BSA)-Epigallocatechin gallate (EGCG) Nanoparticles and Their Transport across Monolayers of Human Intestinal Epithelial Caco-2 Cells Food Funct. 2014 1278 1285
    • (2014) Food Funct. , pp. 1278-1285
    • Li, Z.1    Ha, J.-H.2    Zou, T.3    Gu, L.4
  • 52
    • 84857766775 scopus 로고    scopus 로고
    • Thermally-induced beta-lactoglobulin-EGCG nanovehicles: Loading, stability, sensory and digestive-release study
    • A. Shpigelman Y. Cohen Y. D. Livney Thermally-induced beta-lactoglobulin-EGCG nanovehicles: Loading, stability, sensory and digestive-release study Food Hydrocolloids 2012 29 57 67
    • (2012) Food Hydrocolloids , vol.29 , pp. 57-67
    • Shpigelman, A.1    Cohen, Y.2    Livney, Y.D.3
  • 53
    • 84861573437 scopus 로고    scopus 로고
    • Food protein aggregates as vitamin-matrix carriers: Impact of processing conditions
    • P. Relkin R. Shukat Food protein aggregates as vitamin-matrix carriers: Impact of processing conditions Food Chem. 2012 134 2141 2148
    • (2012) Food Chem. , vol.134 , pp. 2141-2148
    • Relkin, P.1    Shukat, R.2
  • 54
    • 84865718133 scopus 로고    scopus 로고
    • Inhibition of β-carotene degradation in oil-in-water nanoemulsions: Influence of oil-soluble and water-soluble antioxidants
    • C. Qian E. A. Decker H. Xiao D. J. McClements Inhibition of β-carotene degradation in oil-in-water nanoemulsions: Influence of oil-soluble and water-soluble antioxidants Food Chem. 2012 135 1036 1043
    • (2012) Food Chem. , vol.135 , pp. 1036-1043
    • Qian, C.1    Decker, E.A.2    Xiao, H.3    McClements, D.J.4
  • 55
    • 84856212477 scopus 로고    scopus 로고
    • Physical and chemical stability of β-carotene-enriched nanoemulsions: Influence of pH, ionic strength, temperature, and emulsifier type
    • C. Qian E. A. Decker H. Xiao D. J. McClements Physical and chemical stability of β-carotene-enriched nanoemulsions: Influence of pH, ionic strength, temperature, and emulsifier type Food Chem. 2011 132 1221 1229
    • (2011) Food Chem. , vol.132 , pp. 1221-1229
    • Qian, C.1    Decker, E.A.2    Xiao, H.3    McClements, D.J.4
  • 56
    • 84855715840 scopus 로고    scopus 로고
    • Nanoemulsion- and emulsion-based delivery systems for curcumin: Encapsulation and release properties
    • K. Ahmed Y. Li D. J. McClements H. Xiao Nanoemulsion- and emulsion-based delivery systems for curcumin: Encapsulation and release properties Food Chem. 2012 132 799 807
    • (2012) Food Chem. , vol.132 , pp. 799-807
    • Ahmed, K.1    Li, Y.2    McClements, D.J.3    Xiao, H.4
  • 57
    • 31544467034 scopus 로고    scopus 로고
    • Swelling Behavior and Controlled Release of Theophylline and Sulfamethoxazole Drugs in β-Lactoglobulin Protein Gels Obtained by Phase Separation in Water-Ethanol Mixture
    • T. T. Reddy L. Lavenant J. Lefebvre D. Renard Swelling Behavior and Controlled Release of Theophylline and Sulfamethoxazole Drugs in β-Lactoglobulin Protein Gels Obtained by Phase Separation in Water-Ethanol Mixture Biomacromolecules 2005 7 323 330
    • (2005) Biomacromolecules , vol.7 , pp. 323-330
    • Reddy, T.T.1    Lavenant, L.2    Lefebvre, J.3    Renard, D.4
  • 58
    • 73449145946 scopus 로고    scopus 로고
    • In vitro release of α-tocopherol from emulsion-loaded β-lactoglobulin gels
    • L. Liang V. Leung Sok Line G. E. Remondetto M. Subirade In vitro release of α-tocopherol from emulsion-loaded β-lactoglobulin gels Int. Dairy J. 2010 20 176 181
    • (2010) Int. Dairy J. , vol.20 , pp. 176-181
    • Liang, L.1    Leung Sok Line, V.2    Remondetto, G.E.3    Subirade, M.4
  • 59
    • 84861228782 scopus 로고    scopus 로고
    • Enhancing the in vitro Fe2+ bio-accessibility using ascorbate and cold-set whey protein gel particles
    • A. H. Martin G. A. H. de Jong Enhancing the in vitro Fe2+ bio-accessibility using ascorbate and cold-set whey protein gel particles Dairy Sci. Technol. 2012 92 133 149
    • (2012) Dairy Sci. Technol. , vol.92 , pp. 133-149
    • Martin, A.H.1    De Jong, G.A.H.2
  • 60
    • 0036214404 scopus 로고    scopus 로고
    • Cold Gelation of β-lactoglobulin in the Presence of Iron
    • G. E. Remondetto P. Paquin M. Subirade Cold Gelation of β-lactoglobulin in the Presence of Iron J. Food Sci. 2002 67 586 595
    • (2002) J. Food Sci. , vol.67 , pp. 586-595
    • Remondetto, G.E.1    Paquin, P.2    Subirade, M.3
  • 61
    • 84857059676 scopus 로고    scopus 로고
    • Study of the acid and thermal stability of β-lactoglobulin-ligand complexes using fluorescence quenching
    • L. Liang M. Subirade Study of the acid and thermal stability of β-lactoglobulin-ligand complexes using fluorescence quenching Food Chem. 2012 132 2023 2029
    • (2012) Food Chem. , vol.132 , pp. 2023-2029
    • Liang, L.1    Subirade, M.2
  • 62
    • 84890029411 scopus 로고    scopus 로고
    • Milk protein-vitamin interactions: Formation of beta-lactoglobulin/folic acid nano-complexes and their impact on in vitro gastro-duodenal proteolysis
    • O. E. Pérez T. David-Birman E. Kesselman S. Levi-Tal U. Lesmes Milk protein-vitamin interactions: Formation of beta-lactoglobulin/folic acid nano-complexes and their impact on in vitro gastro-duodenal proteolysis Food Hydrocolloids 2014 38 40 47
    • (2014) Food Hydrocolloids , vol.38 , pp. 40-47
    • Pérez, O.E.1    David-Birman, T.2    Kesselman, E.3    Levi-Tal, S.4    Lesmes, U.5
  • 63
    • 84877612967 scopus 로고    scopus 로고
    • Carboxymethyl Chitosan-Soy Protein Complex Nanoparticles for the Encapsulation and Controlled Release of Vitamin D3
    • Z. Teng Y. Luo Q. Wang Carboxymethyl Chitosan-Soy Protein Complex Nanoparticles for the Encapsulation and Controlled Release of Vitamin D3 Food Chem. 2013 141 524 532
    • (2013) Food Chem. , vol.141 , pp. 524-532
    • Teng, Z.1    Luo, Y.2    Wang, Q.3
  • 64
    • 84863362655 scopus 로고    scopus 로고
    • Nanoparticles Synthesized from Soy Protein: Preparation, Characterization, and Application for Nutraceutical Encapsulation
    • Z. Teng Y. C. Luo Q. Wang Nanoparticles Synthesized from Soy Protein: Preparation, Characterization, and Application for Nutraceutical Encapsulation J. Agric. Food Chem. 2012 60 2712 2720
    • (2012) J. Agric. Food Chem. , vol.60 , pp. 2712-2720
    • Teng, Z.1    Luo, Y.C.2    Wang, Q.3
  • 65
    • 75149130837 scopus 로고    scopus 로고
    • Preparation of nanoparticles from denatured whey protein by pH-cycling treatment
    • H. J. Giroux J. Houde M. Britten Preparation of nanoparticles from denatured whey protein by pH-cycling treatment Food Hydrocolloids 2009 24 341 346
    • (2009) Food Hydrocolloids , vol.24 , pp. 341-346
    • Giroux, H.J.1    Houde, J.2    Britten, M.3
  • 66
    • 84864779299 scopus 로고    scopus 로고
    • Nanoparticle surface charge mediates the cellular receptors used by protein-nanoparticle complexes
    • C. C. Fleischer C. K. Payne Nanoparticle surface charge mediates the cellular receptors used by protein-nanoparticle complexes J. Phys. Chem. B 2012 116 8901 8907
    • (2012) J. Phys. Chem. B , vol.116 , pp. 8901-8907
    • Fleischer, C.C.1    Payne, C.K.2
  • 67
    • 33847391136 scopus 로고    scopus 로고
    • Preparation of sub-100-nm beta-lactoglobulin (BLG) nanoparticles
    • S. Ko S. Gunasekaran Preparation of sub-100-nm beta-lactoglobulin (BLG) nanoparticles J. Microencapsulation 2006 23 887 898
    • (2006) J. Microencapsulation , vol.23 , pp. 887-898
    • Ko, S.1    Gunasekaran, S.2
  • 68
    • 84859395894 scopus 로고    scopus 로고
    • Preservation of (-)-Epigallocatechin-3-gallate Antioxidant Properties Loaded in Heat Treated β-Lactoglobulin Nanoparticles
    • B. Li W. Du J. Jin Q. Du Preservation of (-)-Epigallocatechin-3-gallate Antioxidant Properties Loaded in Heat Treated β-Lactoglobulin Nanoparticles J. Agric. Food Chem. 2012 60 3477 3484
    • (2012) J. Agric. Food Chem. , vol.60 , pp. 3477-3484
    • Li, B.1    Du, W.2    Jin, J.3    Du, Q.4
  • 69
    • 77957724075 scopus 로고    scopus 로고
    • Biorelevant Dissolution Methods and Their Applications in In Vitro-In Vivo Correlations for Oral Formulations
    • N. Fotaki M. Vertzoni Biorelevant Dissolution Methods and Their Applications in In Vitro-In Vivo Correlations for Oral Formulations Open Drug Delivery J. 2010 4 2 13
    • (2010) Open Drug Delivery J. , vol.4 , pp. 2-13
    • Fotaki, N.1    Vertzoni, M.2
  • 70
    • 84908325535 scopus 로고    scopus 로고
    • Enhancement of aqueous stability of allyl isothiocyanate using nanoemulsions prepared by an emulsion inversion point method
    • Y. Li Z. Teng P. Chen Y. Song Y. Luo Q. Wang Enhancement of aqueous stability of allyl isothiocyanate using nanoemulsions prepared by an emulsion inversion point method J. Colloid Interface Sci. 2015 438 130 137
    • (2015) J. Colloid Interface Sci. , vol.438 , pp. 130-137
    • Li, Y.1    Teng, Z.2    Chen, P.3    Song, Y.4    Luo, Y.5    Wang, Q.6
  • 72
    • 84856719507 scopus 로고    scopus 로고
    • Nanoemulsions versus microemulsions: Terminology, differences, and similarities
    • D. J. McClements Nanoemulsions versus microemulsions: terminology, differences, and similarities Soft Matter 2012 8 1719 1729
    • (2012) Soft Matter , vol.8 , pp. 1719-1729
    • McClements, D.J.1
  • 73
    • 78650539714 scopus 로고    scopus 로고
    • Self-nanoemulsifying drug delivery systems: Formulation insights, applications and advances
    • A. A. Date N. Desai R. Dixit M. Nagarsenker Self-nanoemulsifying drug delivery systems: formulation insights, applications and advances Nanomedicine 2010 5 1595 1616
    • (2010) Nanomedicine , vol.5 , pp. 1595-1616
    • Date, A.A.1    Desai, N.2    Dixit, R.3    Nagarsenker, M.4
  • 74
    • 84908325535 scopus 로고    scopus 로고
    • Enhancement of aqueous stability of allyl isothiocyanate using nanoemulsions prepared by an emulsion inversion point method
    • Y. Li Z. Teng P. Chen Y. Song Y. Luo Q. Wang Enhancement of aqueous stability of allyl isothiocyanate using nanoemulsions prepared by an emulsion inversion point method J. Colloid Interface Sci. 2015 438 130 137
    • (2015) J. Colloid Interface Sci. , vol.438 , pp. 130-137
    • Li, Y.1    Teng, Z.2    Chen, P.3    Song, Y.4    Luo, Y.5    Wang, Q.6
  • 75
    • 0002609034 scopus 로고
    • Relationships of hydrophobicity to emulsifying properties of heat denatured proteins
    • L. P. Voutsinas E. Cheung S. Nakai Relationships of hydrophobicity to emulsifying properties of heat denatured proteins J. Food Sci. 1983 48 26 32
    • (1983) J. Food Sci. , vol.48 , pp. 26-32
    • Voutsinas, L.P.1    Cheung, E.2    Nakai, S.3
  • 76
    • 0345711506 scopus 로고    scopus 로고
    • Surface functional properties of native, acid-treated, and reduced soy glycinin. 2. Emulsifying properties
    • J. R. Wagner J. Gueguen Surface functional properties of native, acid-treated, and reduced soy glycinin. 2. Emulsifying properties J. Agric. Food Chem. 1999 47 2181 2187
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 2181-2187
    • Wagner, J.R.1    Gueguen, J.2
  • 77
    • 0034001548 scopus 로고    scopus 로고
    • Comparison of protein surface hydrophobicity measured at various pH values using three different fluorescent probes
    • N. Alizadeh-Pasdar E. C. Y. Li-Chan Comparison of protein surface hydrophobicity measured at various pH values using three different fluorescent probes J. Agric. Food Chem. 2000 48 328 334
    • (2000) J. Agric. Food Chem. , vol.48 , pp. 328-334
    • Alizadeh-Pasdar, N.1    Li-Chan, E.C.Y.2
  • 78
    • 0019331914 scopus 로고
    • Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins
    • A. Kato S. Nakai Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins Biochim. Biophys. Acta, Protein Struct. 1980 624 13 20
    • (1980) Biochim. Biophys. Acta, Protein Struct. , vol.624 , pp. 13-20
    • Kato, A.1    Nakai, S.2
  • 79
    • 67649939005 scopus 로고    scopus 로고
    • Emulsification alters simulated gastrointestinal proteolysis of β-casein and β-lactoglobulin
    • A. Macierzanka A. I. Sancho E. N. C. Mills N. M. Rigby A. R. Mackie Emulsification alters simulated gastrointestinal proteolysis of β-casein and β-lactoglobulin Soft Matter 2009 5 538 550
    • (2009) Soft Matter , vol.5 , pp. 538-550
    • Macierzanka, A.1    Sancho, A.I.2    Mills, E.N.C.3    Rigby, N.M.4    Mackie, A.R.5
  • 82
    • 84870807825 scopus 로고    scopus 로고
    • Development of carboxymethyl chitosan hydrogel beads in alcohol-aqueous binary solvent for nutrient delivery applications
    • Y. Luo Z. Teng X. Wang Q. Wang Development of carboxymethyl chitosan hydrogel beads in alcohol-aqueous binary solvent for nutrient delivery applications Food Hydrocolloids 2013 31 332 339
    • (2013) Food Hydrocolloids , vol.31 , pp. 332-339
    • Luo, Y.1    Teng, Z.2    Wang, X.3    Wang, Q.4
  • 83
    • 0002593957 scopus 로고
    • Calcium binding and salt-induced structural changes of native and preheated beta-lactoglobulin
    • S. Jeyarajah J. C. Allen Calcium binding and salt-induced structural changes of native and preheated beta-lactoglobulin J. Agric. Food Chem. 1994 42 80 85
    • (1994) J. Agric. Food Chem. , vol.42 , pp. 80-85
    • Jeyarajah, S.1    Allen, J.C.2
  • 84
    • 84875924891 scopus 로고    scopus 로고
    • Encapsulation of indole-3-carbinol and 3,3′-diindolylmethane in zein/carboxymethyl chitosan nanoparticles with controlled release property and improved stability
    • Y. Luo T. Wang Z. Teng P. Chen J. Sun Q. Wang Encapsulation of indole-3-carbinol and 3,3′-diindolylmethane in zein/carboxymethyl chitosan nanoparticles with controlled release property and improved stability Food Chem. 2013 139 224 230
    • (2013) Food Chem. , vol.139 , pp. 224-230
    • Luo, Y.1    Wang, T.2    Teng, Z.3    Chen, P.4    Sun, J.5    Wang, Q.6
  • 85
    • 84896939359 scopus 로고    scopus 로고
    • Tangeretin-loaded protein nanoparticles fabricated from zein/β-lactoglobulin: Preparation, characterization, and functional performance
    • J. Chen J. Zheng D. J. McClements H. Xiao Tangeretin-loaded protein nanoparticles fabricated from zein/β-lactoglobulin: Preparation, characterization, and functional performance Food Chem. 2014 158 466 472
    • (2014) Food Chem. , vol.158 , pp. 466-472
    • Chen, J.1    Zheng, J.2    McClements, D.J.3    Xiao, H.4
  • 86
    • 80052501915 scopus 로고    scopus 로고
    • Recent progress in biopolymer nanoparticle and microparticle formation by heat-treating electrostatic protein-polysaccharide complexes
    • O. G. Jones D. J. McClements Recent progress in biopolymer nanoparticle and microparticle formation by heat-treating electrostatic protein-polysaccharide complexes Adv. Colloid Interface Sci. 2011 167 49 62
    • (2011) Adv. Colloid Interface Sci. , vol.167 , pp. 49-62
    • Jones, O.G.1    McClements, D.J.2
  • 87
    • 84908519080 scopus 로고    scopus 로고
    • Self-assembly of β-lactoglobulin and egg white lysozyme as a potential carrier for nutraceuticals
    • F. Diarrassouba G. Remondetto G. Garrait P. Alvarez E. Beyssac M. Subirade Self-assembly of β-lactoglobulin and egg white lysozyme as a potential carrier for nutraceuticals Food Chem. 2015 173 203 209
    • (2015) Food Chem. , vol.173 , pp. 203-209
    • Diarrassouba, F.1    Remondetto, G.2    Garrait, G.3    Alvarez, P.4    Beyssac, E.5    Subirade, M.6
  • 88
    • 34447632834 scopus 로고    scopus 로고
    • Formation of hydrogel particles by thermal treatment of β-lactoglobulin-chitosan complexes
    • Y.-H. Hong D. J. McClements Formation of hydrogel particles by thermal treatment of β-lactoglobulin-chitosan complexes J. Agric. Food Chem. 2007 55 5653 5660
    • (2007) J. Agric. Food Chem. , vol.55 , pp. 5653-5660
    • Hong, Y.-H.1    McClements, D.J.2
  • 89
    • 84875670462 scopus 로고    scopus 로고
    • Formation and characterization of quercetin-loaded chitosan oligosaccharide/β-lactoglobulin nanoparticle
    • H.-K. Ha J. W. Kim M.-R. Lee W.-J. Lee Formation and characterization of quercetin-loaded chitosan oligosaccharide/β-lactoglobulin nanoparticle Food Res. Int. 2013 52 82 90
    • (2013) Food Res. Int. , vol.52 , pp. 82-90
    • Ha, H.-K.1    Kim, J.W.2    Lee, M.-R.3    Lee, W.-J.4
  • 90
    • 77955511339 scopus 로고    scopus 로고
    • Beta-lactoglobulin-polysaccharide complexes as nanovehicles for hydrophobic nutraceuticals in non-fat foods and clear beverages
    • N. Ron P. Zimet J. Bargarum Y. D. Livney Beta-lactoglobulin-polysaccharide complexes as nanovehicles for hydrophobic nutraceuticals in non-fat foods and clear beverages Int. Dairy J. 2010 20 686 693
    • (2010) Int. Dairy J. , vol.20 , pp. 686-693
    • Ron, N.1    Zimet, P.2    Bargarum, J.3    Livney, Y.D.4
  • 91
    • 76049130071 scopus 로고    scopus 로고
    • Comparison of protein-polysaccharide nanoparticle fabrication methods: Impact of biopolymer complexation before or after particle formation
    • O. G. Jones E. A. Decker D. J. McClements Comparison of protein-polysaccharide nanoparticle fabrication methods: Impact of biopolymer complexation before or after particle formation J. Colloid Interface Sci. 2010 344 21 29
    • (2010) J. Colloid Interface Sci. , vol.344 , pp. 21-29
    • Jones, O.G.1    Decker, E.A.2    McClements, D.J.3
  • 92
    • 84894270014 scopus 로고    scopus 로고
    • β-Lactoglobulin-carboxymethylcellulose core-shell microparticles: Construction, characterization and isolation
    • L. Carpineti M. J. Martinez A. M. Pilosof O. E. Pérez β-Lactoglobulin-carboxymethylcellulose core-shell microparticles: Construction, characterization and isolation J. Food Eng. 2014 131 65 74
    • (2014) J. Food Eng. , vol.131 , pp. 65-74
    • Carpineti, L.1    Martinez, M.J.2    Pilosof, A.M.3    Pérez, O.E.4
  • 93
    • 0242489071 scopus 로고    scopus 로고
    • Protection of bifidobacteria encapsulated in polysaccharide-protein gel beads against gastric juice and bile
    • D. Guérin J.-C. Vuillemard M. Subirade Protection of bifidobacteria encapsulated in polysaccharide-protein gel beads against gastric juice and bile J. Food Prot. 2003 66 2076 2084
    • (2003) J. Food Prot. , vol.66 , pp. 2076-2084
    • Guérin, D.1    Vuillemard, J.-C.2    Subirade, M.3
  • 94
    • 4444274244 scopus 로고    scopus 로고
    • Influence of pH and carrageenan type on properties of β-lactoglobulin stabilized oil-in-water emulsions
    • Y. S. Gu E. A. Decker D. J. McClements Influence of pH and carrageenan type on properties of β-lactoglobulin stabilized oil-in-water emulsions Food Hydrocolloids 2005 19 83 91
    • (2005) Food Hydrocolloids , vol.19 , pp. 83-91
    • Gu, Y.S.1    Decker, E.A.2    McClements, D.J.3
  • 95
    • 4043129561 scopus 로고    scopus 로고
    • Factors influencing the production of o/w emulsions stabilized by β-lactoglobulin-pectin membranes
    • D. Guzey H. Kim D. J. McClements Factors influencing the production of o/w emulsions stabilized by β-lactoglobulin-pectin membranes Food Hydrocolloids 2004 18 967 975
    • (2004) Food Hydrocolloids , vol.18 , pp. 967-975
    • Guzey, D.1    Kim, H.2    McClements, D.J.3
  • 96
    • 84906875682 scopus 로고    scopus 로고
    • Controlled Release of β-Carotene in β-Lactoglobulin-Dextran-Conjugated Nanoparticles' in Vitro Digestion and Transport with Caco-2 Monolayers
    • J. Yi T. I. Lam W. Yokoyama L. W. Cheng F. Zhong Controlled Release of β-Carotene in β-Lactoglobulin-Dextran-Conjugated Nanoparticles' in Vitro Digestion and Transport with Caco-2 Monolayers J. Agric. Food Chem. 2014 62 8900 8907
    • (2014) J. Agric. Food Chem. , vol.62 , pp. 8900-8907
    • Yi, J.1    Lam, T.I.2    Yokoyama, W.3    Cheng, L.W.4    Zhong, F.5
  • 97
    • 79961171984 scopus 로고    scopus 로고
    • Controlling lipid digestibility: Response of lipid droplets coated by β-lactoglobulin-dextran Maillard conjugates to simulated gastrointestinal conditions
    • U. Lesmes D. J. McClements Controlling lipid digestibility: Response of lipid droplets coated by β-lactoglobulin-dextran Maillard conjugates to simulated gastrointestinal conditions Food Hydrocolloids 2012 26 221 230
    • (2012) Food Hydrocolloids , vol.26 , pp. 221-230
    • Lesmes, U.1    McClements, D.J.2
  • 98
    • 84897458656 scopus 로고    scopus 로고
    • Cationic β-lactoglobulin nanoparticles as a bioavailability enhancer: Comparison between ethylenediamine and polyethyleneimine as cationizers
    • Z. Teng Y. Li Y. Niu Y. Xu L. Yu Q. Wang Cationic β-lactoglobulin nanoparticles as a bioavailability enhancer: Comparison between ethylenediamine and polyethyleneimine as cationizers Food Chem. 2014 159 333 342
    • (2014) Food Chem. , vol.159 , pp. 333-342
    • Teng, Z.1    Li, Y.2    Niu, Y.3    Xu, Y.4    Yu, L.5    Wang, Q.6
  • 99
    • 0000746555 scopus 로고
    • Physicochemical and functional properties of positively charged derivatives of bovine beta-lactoglobulin
    • N. L. Mattarella T. Richardson Physicochemical and functional properties of positively charged derivatives of bovine beta-lactoglobulin J. Agric. Food Chem. 1983 31 972 978
    • (1983) J. Agric. Food Chem. , vol.31 , pp. 972-978
    • Mattarella, N.L.1    Richardson, T.2
  • 100
    • 0038321352 scopus 로고    scopus 로고
    • The natural history of food allergy
    • R. A. Wood The natural history of food allergy Pediatrics 2003 111 1631 1637
    • (2003) Pediatrics , vol.111 , pp. 1631-1637
    • Wood, R.A.1
  • 101
    • 0034941083 scopus 로고    scopus 로고
    • Cow's milk protein allergy and possible means for its prevention
    • B.-M. Exl R. Fritsché Cow's milk protein allergy and possible means for its prevention Nutrition 2001 17 642 651
    • (2001) Nutrition , vol.17 , pp. 642-651
    • Exl, B.-M.1    Fritsché, R.2
  • 104
    • 84862788892 scopus 로고    scopus 로고
    • Preparation and in vitro evaluation of calcium-induced soy protein isolate nanoparticles and their formation mechanism study
    • J. Zhang L. Liang Z. Tian L. Chen M. Subirade Preparation and in vitro evaluation of calcium-induced soy protein isolate nanoparticles and their formation mechanism study Food Chem. 2012 133 390 399
    • (2012) Food Chem. , vol.133 , pp. 390-399
    • Zhang, J.1    Liang, L.2    Tian, Z.3    Chen, L.4    Subirade, M.5
  • 105
    • 1542286920 scopus 로고    scopus 로고
    • Modification of IgE Binding during Heat Processing of the Cow's Milk Allergen β-Lactoglobulin
    • B.-M. Ehn B. Ekstrand U. Bengtsson S. Ahlstedt Modification of IgE Binding during Heat Processing of the Cow's Milk Allergen β-Lactoglobulin J. Agric. Food Chem. 2004 52 1398 1403
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 1398-1403
    • Ehn, B.-M.1    Ekstrand, B.2    Bengtsson, U.3    Ahlstedt, S.4
  • 106
    • 0000016467 scopus 로고    scopus 로고
    • Effect of polysaccharide conjugation or transglutaminase treatment on the allergenicity and functional properties of soy protein
    • E. F. E. Babiker A. Hiroyuki N. Matsudomi H. Iwata T. Ogawa N. Bando A. Kato Effect of polysaccharide conjugation or transglutaminase treatment on the allergenicity and functional properties of soy protein J. Agric. Food Chem. 1998 46 866 871
    • (1998) J. Agric. Food Chem. , vol.46 , pp. 866-871
    • Babiker, E.F.E.1    Hiroyuki, A.2    Matsudomi, N.3    Iwata, H.4    Ogawa, T.5    Bando, N.6    Kato, A.7
  • 107
    • 84928340288 scopus 로고    scopus 로고
    • NTP Technical Report on Toxicity Studies of Glutaraldehyde Administered by Inhalation to F344/N Rats and B6C3F 1 Mice. NIH Publication 93-3348, dated March 1993. US Department of Health and Human Services. In National Toxicology Program: 1993
    • NTP Technical Report on Toxicity Studies of Glutaraldehyde Administered by Inhalation to F344/N Rats and B6C3F 1 Mice. NIH Publication 93-3348, dated March 1993. US Department of Health and Human Services. In National Toxicology Program: 1993
  • 108
    • 1842739438 scopus 로고    scopus 로고
    • A novel pH-sensitive hydrogel composed of N,O-carboxymethyl chitosan and alginate cross-linked by genipin for protein drug delivery
    • S.-C. Chen Y.-C. Wu F.-L. Mi Y.-H. Lin L.-C. Yu H.-W. Sung A novel pH-sensitive hydrogel composed of N,O-carboxymethyl chitosan and alginate cross-linked by genipin for protein drug delivery J. Controlled Release 2004 96 285 300
    • (2004) J. Controlled Release , vol.96 , pp. 285-300
    • Chen, S.-C.1    Wu, Y.-C.2    Mi, F.-L.3    Lin, Y.-H.4    Yu, L.-C.5    Sung, H.-W.6
  • 109
    • 0001299616 scopus 로고
    • Enzymic modification of proteins: Effects of transglutaminase cross-linking on some physical properties of beta-lactoglobulin
    • S. Y. Tanimoto J. E. Kinsella Enzymic modification of proteins: effects of transglutaminase cross-linking on some physical properties of beta-lactoglobulin J. Agric. Food Chem. 1988 36 281 285
    • (1988) J. Agric. Food Chem. , vol.36 , pp. 281-285
    • Tanimoto, S.Y.1    Kinsella, J.E.2
  • 110
    • 0642362759 scopus 로고    scopus 로고
    • Cross-linking of milk proteins with transglutaminase at the oil-water interface
    • M. Fargemand B. S. Murray E. Dickinson Cross-linking of milk proteins with transglutaminase at the oil-water interface J. Agric. Food Chem. 1997 45 2514 2519
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 2514-2519
    • Fargemand, M.1    Murray, B.S.2    Dickinson, E.3
  • 111
    • 84897691215 scopus 로고    scopus 로고
    • Nanodelivery of bioactive components for food applications: Types of delivery systems, properties, and their effect on ADME profiles and toxicity of nanoparticles
    • T. Borel C. M. Sabliov Nanodelivery of bioactive components for food applications: types of delivery systems, properties, and their effect on ADME profiles and toxicity of nanoparticles Annu. Rev. Food Sci. Technol. 2014 5 197 213
    • (2014) Annu. Rev. Food Sci. Technol. , vol.5 , pp. 197-213
    • Borel, T.1    Sabliov, C.M.2
  • 112
    • 84874995378 scopus 로고    scopus 로고
    • Development and Application of Nanoparticles Synthesized with Folic Acid Conjugated Soy Protein
    • Z. Teng Y. Luo T. Wang B. Zhang Q. Wang Development and Application of Nanoparticles Synthesized with Folic Acid Conjugated Soy Protein J. Agric. Food Chem. 2013 61 2556 2564
    • (2013) J. Agric. Food Chem. , vol.61 , pp. 2556-2564
    • Teng, Z.1    Luo, Y.2    Wang, T.3    Zhang, B.4    Wang, Q.5
  • 113
    • 52149109329 scopus 로고    scopus 로고
    • Colloidal delivery systems for micronutrients and nutraceuticals
    • K. P. Velikov E. Pelan Colloidal delivery systems for micronutrients and nutraceuticals Soft Matter 2008 4 1964 1980
    • (2008) Soft Matter , vol.4 , pp. 1964-1980
    • Velikov, K.P.1    Pelan, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.