메뉴 건너뛰기




Volumn 33, Issue 1, 2013, Pages 67-74

Production and characterization of beta-lactoglobulin/alginate nanoemulsion containing coenzyme Q10: Impact of heat treatment and alginate concentrate

Author keywords

lactoglobulin; Alginate; Coenzyme Q10; Nanoemulsion

Indexed keywords


EID: 84884650556     PISSN: 12258563     EISSN: None     Source Type: Journal    
DOI: 10.5851/kosfa.2013.33.1.67     Document Type: Article
Times cited : (12)

References (36)
  • 2
    • 84893617475 scopus 로고
    • Ca2+-induced gelation of pre-heated whey protein isolate
    • Barbut, S. and Foegeding, E. A. (1993) Ca2+-induced gelation of pre-heated whey protein isolate. Food Sci. 58, 867-871.
    • (1993) Food Sci. , vol.58 , pp. 867-871
    • Barbut, S.1    Foegeding, E.A.2
  • 3
    • 0036196485 scopus 로고    scopus 로고
    • Elaboration and characterization of whey protein beads by an emulsification/cold gelation process: Application for the protection of retinol
    • Beaulieu, L., Savoie, L., Paquin, P., and Subirade, M. (2002) Elaboration and characterization of whey protein beads by an emulsification/cold gelation process: Application for the protection of retinol. Biomacromolecule. 3, 239-248.
    • (2002) Biomacromolecule. , vol.3 , pp. 239-248
    • Beaulieu, L.1    Savoie, L.2    Paquin, P.3    Subirade, M.4
  • 4
    • 3242721638 scopus 로고    scopus 로고
    • Nano-emulsion formulation using spontaneous emulsification: Solvent, oil and surfactant optimization
    • Bouchemal, K., Briancon, S., Perrier, E., and Fessi, H. (2004) Nano-emulsion formulation using spontaneous emulsification: solvent, oil and surfactant optimization. Int. J. Pharm. 280, 241-251.
    • (2004) Int. J. Pharm. , vol.280 , pp. 241-251
    • Bouchemal, K.1    Briancon, S.2    Perrier, E.3    Fessi, H.4
  • 5
    • 33646008554 scopus 로고    scopus 로고
    • Food protein-based materials as nutraceutical delivery systems
    • Chen, L., Remondetto, G. E., and Subirade, M. (2006) Food protein-based materials as nutraceutical delivery systems. Trends Food Sci. Technol. 17, 272-283.
    • (2006) Trends Food Sci. Technol. , vol.17 , pp. 272-283
    • Chen, L.1    Remondetto, G.E.2    Subirade, M.3
  • 6
    • 33744464045 scopus 로고    scopus 로고
    • Alginate-whey protein granular microspheres as oral delivery vehicles for bioactive compounds
    • Chen, L. and Subirade, M. (2006) Alginate-whey protein granular microspheres as oral delivery vehicles for bioactive compounds. Biomaterials 27, 4646-4654.
    • (2006) Biomaterials , vol.27 , pp. 4646-4654
    • Chen, L.1    Subirade, M.2
  • 7
    • 0035667921 scopus 로고    scopus 로고
    • Biochemical functions of coenzyme Q10
    • Crane, F. L. (2001) Biochemical functions of coenzyme Q10. J. Am. Coll. Nutr. 20, 591-598.
    • (2001) J. Am. Coll. Nutr. , vol.20 , pp. 591-598
    • Crane, F.L.1
  • 8
    • 0001042101 scopus 로고    scopus 로고
    • Amino acids, peptides and proteins
    • Fennema, O. R. (3rd ed) Marcel Dekker, Inc., NY
    • Damodaran, S. (1996) Amino acids, peptides and proteins. In: Food chemistry. Fennema, O. R. (3rd ed) Marcel Dekker, Inc., NY, pp. 321-429.
    • (1996) Food Chemistry , pp. 321-429
    • Damodaran, S.1
  • 9
    • 0000618751 scopus 로고
    • Effect of denaturation of β-lactoglobulin on texture properties of set-style nonfat yoghurt. 1. Syneresis
    • Dannenberg, F. and Kessler, H. G. (1988) Effect of denaturation of β-lactoglobulin on texture properties of set-style nonfat yoghurt. 1. Syneresis. Milchwissenschaft 43, 632-635.
    • (1988) Milchwissenschaft , vol.43 , pp. 632-635
    • Dannenberg, F.1    Kessler, H.G.2
  • 10
    • 70649098157 scopus 로고    scopus 로고
    • Surface charged temoporfin-loaded flexible vesicles: In vitro skin penetration studies and stability
    • Dragicevic-Curic, N., Gräfe, S., Gitter, B., Winter, S., and Fahr, A. (2010) Surface charged temoporfin-loaded flexible vesicles: In vitro skin penetration studies and stability. Int. J. Pharm. 384, 100-108.
    • (2010) Int. J. Pharm. , vol.384 , pp. 100-108
    • Dragicevic-Curic, N.1    Gräfe, S.2    Gitter, B.3    Winter, S.4    Fahr, A.5
  • 11
    • 0033802248 scopus 로고    scopus 로고
    • Aggregation kinetics of heated whey protein-stabilized emulsions
    • Euston, S. R., Finnigan, S. R., and Hirst, R. L. (2000) Aggregation kinetics of heated whey protein-stabilized emulsions. Food Hydrocolloid. 14, 155-161.
    • (2000) Food Hydrocolloid. , vol.14 , pp. 155-161
    • Euston, S.R.1    Finnigan, S.R.2    Hirst, R.L.3
  • 12
    • 33746474818 scopus 로고    scopus 로고
    • Polyionic hydrocolloids for the intestinal delivery of protein drugs: Alginate and chitosan - A review
    • George, M. and Abraham, T. E. (2006) Polyionic hydrocolloids for the intestinal delivery of protein drugs: Alginate and chitosan - a review. J. Control. Release 114, 1-14.
    • (2006) J. Control. Release , vol.114 , pp. 1-14
    • George, M.1    Abraham, T.E.2
  • 13
    • 32944461715 scopus 로고    scopus 로고
    • Characterization of β-lactoglobulin-sodium alginate interactions in aqueous solutions: A calorimetry, light scattering, electrophoretic mobility and solubility study
    • Harnsilawat, T., Pongsawatmanit, R., and McClements, D. J. (2006) Characterization of β-lactoglobulin-sodium alginate interactions in aqueous solutions: A calorimetry, light scattering, electrophoretic mobility and solubility study. Food Hydrocolloid. 20, 577-585.
    • (2006) Food Hydrocolloid. , vol.20 , pp. 577-585
    • Harnsilawat, T.1    Pongsawatmanit, R.2    McClements, D.J.3
  • 14
    • 0030919028 scopus 로고    scopus 로고
    • Protein and salt effects on Ca2+-induced cold gelation of whey protein isolate
    • Hongsprabhas, P. and Barbut, S. (1997) Protein and salt effects on Ca2+-induced cold gelation of whey protein isolate. J. Food Sci. 62, 382-385.
    • (1997) J. Food Sci. , vol.62 , pp. 382-385
    • Hongsprabhas, P.1    Barbut, S.2
  • 15
    • 77951442506 scopus 로고    scopus 로고
    • Techniques for efficient entrapment of pharmaceuticals in biodegradable solid micro/nanoparticles
    • Ishihara, T. and Mizushima, T. (2010) Techniques for efficient entrapment of pharmaceuticals in biodegradable solid micro/nanoparticles. Expert Opin. Drug Del. 7, 565-575.
    • (2010) Expert Opin. Drug Del. , vol.7 , pp. 565-575
    • Ishihara, T.1    Mizushima, T.2
  • 16
    • 0037039626 scopus 로고    scopus 로고
    • Formation and stability of nano emulsions prepared using the phase inversion temperature method
    • Izquierdo, P., Esquena, J., Tadros, T. F., Dederen, C., Garcia, M. J. N., Azemar, and Solans, C. (2002) Formation and stability of nano emulsions prepared using the phase inversion temperature method. Langmuir 18, 26-30.
    • (2002) Langmuir , vol.18 , pp. 26-30
    • Izquierdo, P.1    Esquena, J.2    Tadros, T.F.3    Dederen, C.4    Azemar, N.J.G.M.5    Solans, C.6
  • 17
    • 28444497806 scopus 로고    scopus 로고
    • Influence of EDTA and citrate on thermal stability of whey protein stabilized oil-in-water emulsions containing calcium chloride
    • Keowmaneechai, E. and McClements, D. J. (2006) Influence of EDTA and citrate on thermal stability of whey protein stabilized oil-in-water emulsions containing calcium chloride. Food Res. Int. 39, 230-239.
    • (2006) Food Res. Int. , vol.39 , pp. 230-239
    • Keowmaneechai, E.1    McClements, D.J.2
  • 18
    • 0037121041 scopus 로고    scopus 로고
    • Preparation and characterization of coenzyme Q10-loaded PMMA nanoparticles by a new emulsification process based on microfluidization
    • Kwon, S. S., Nam, Y. S., Lee, J. S., Ku, B. S., Han, S. H., Lee, J. Y., and Chang, I. S. (2002) Preparation and characterization of coenzyme Q10-loaded PMMA nanoparticles by a new emulsification process based on microfluidization. Coll. Surf. A: physicochem. eng. Aspects. 210, 95-104.
    • (2002) Coll. Surf. A: Physicochem. Eng. Aspects. , vol.210 , pp. 95-104
    • Kwon, S.S.1    Nam, Y.S.2    Lee, J.S.3    Ku, B.S.4    Han, S.H.5    Lee, J.Y.6    Chang, I.S.7
  • 20
    • 38849129380 scopus 로고    scopus 로고
    • Interaction of β-lactoglobulin with resveratrol and its biological implications
    • Liang, L., Tajmir-Riahi, H. A., and Subirade, M. (2008) Interaction of β-lactoglobulin with resveratrol and its biological implications. Biomacromolecule. 9, 50-56.
    • (2008) Biomacromolecule. , vol.9 , pp. 50-56
    • Liang, L.1    Tajmir-Riahi, H.A.2    Subirade, M.3
  • 21
    • 8644288237 scopus 로고    scopus 로고
    • Cold gelation of β-lactoglobulin oil-in-water emulsions
    • Line, V. L. S., Remondetto, G. E., and Subirade, M. (2005) Cold gelation of β-lactoglobulin oil-in-water emulsions. Food Hydrocolloid. 19, 269-278.
    • (2005) Food Hydrocolloid. , vol.19 , pp. 269-278
    • Line, V.L.S.1    Remondetto, G.E.2    Subirade, M.3
  • 22
    • 75849156917 scopus 로고    scopus 로고
    • Milk proteins as vehicles for bioactives
    • Livney, Y. D. (2010) Milk proteins as vehicles for bioactives. Curr. Opin. Colloid Interface Sci. 15, 73-83.
    • (2010) Curr. Opin. Colloid Interface Sci. , vol.15 , pp. 73-83
    • Livney, Y.D.1
  • 23
    • 35348900910 scopus 로고    scopus 로고
    • Emulsion- based delivery systems for lipophilic bioactive components
    • McClements, D. J., Decker, E. A., and Weiss, J. (2007) Emulsion- based delivery systems for lipophilic bioactive components. J. Food Sci. 72, R109-R124.
    • (2007) J. Food Sci. , vol.72
    • McClements, D.J.1    Decker, E.A.2    Weiss, J.3
  • 24
    • 0002915720 scopus 로고
    • Effect of pH and temperature on protein unfolding and thiol/ disulfide interchange reactions during heat-induced gelation of whey proteins
    • Monahan, F. J., German, J. B., and Kinsella, J. E. (1995) Effect of pH and temperature on protein unfolding and thiol/ disulfide interchange reactions during heat-induced gelation of whey proteins. J. Agric. Food Chem. 43, 46-52.
    • (1995) J. Agric. Food Chem. , vol.43 , pp. 46-52
    • Monahan, F.J.1    German, J.B.2    Kinsella, J.E.3
  • 25
    • 0034774241 scopus 로고    scopus 로고
    • Hydrophobicity of whey protein concentrates measured by fluorescence quenching and its relation with surface functional properties
    • Moro, A., Gatti, C., and Delorenzi, N. (2001) Hydrophobicity of whey protein concentrates measured by fluorescence quenching and its relation with surface functional properties. J. Agric. Food Chem. 49, 4784-4789.
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 4784-4789
    • Moro, A.1    Gatti, C.2    Delorenzi, N.3
  • 26
    • 75149162776 scopus 로고    scopus 로고
    • Effect of heat treatment on milk protein functionality at emulsion interfaces. A review
    • Raikos, V. (2010) Effect of heat treatment on milk protein functionality at emulsion interfaces. A review. Food Hydrocolloid. 24, 259-265.
    • (2010) Food Hydrocolloid. , vol.24 , pp. 259-265
    • Raikos, V.1
  • 27
    • 77955511339 scopus 로고    scopus 로고
    • Beta-lactoglobulin-polysaccharide complexes as nanovehicles for hydrophobic nutraceuticals in non-fat foods and clear beverages
    • Ron, N., Zimet, P., Bargarum, J., and Livney, Y. D. (2010) Beta-lactoglobulin-polysaccharide complexes as nanovehicles for hydrophobic nutraceuticals in non-fat foods and clear beverages. Int. Dairy J. 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
  • 28
    • 67651115509 scopus 로고    scopus 로고
    • Multiscale characterization of individualized β-lactoglobulin mcirogels formed upon heat treatment under narrow pH range conditions
    • Schmitt, C., Bovay, C., Vuilliomenet, A. M., Rouvet, M., Bovetto, L., Barbar, R., and Sanchez, C. (2009) Multiscale characterization of individualized β-lactoglobulin mcirogels formed upon heat treatment under narrow pH range conditions. Langmuir 25, 7899-7909.
    • (2009) Langmuir , vol.25 , pp. 7899-7909
    • Schmitt, C.1    Bovay, C.2    Vuilliomenet, A.M.3    Rouvet, M.4    Bovetto, L.5    Barbar, R.6    Sanchez, C.7
  • 29
    • 0000361334 scopus 로고
    • Effect of processing on whey protein functionality
    • Schmidt, R. H., Packard, V. S., and Morris, H. A. (1984) Effect of processing on whey protein functionality. J. Dairy Sci. 67, 2723-2733.
    • (1984) J. Dairy Sci. , vol.67 , pp. 2723-2733
    • Schmidt, R.H.1    Packard, V.S.2    Morris, H.A.3
  • 32
    • 84862954537 scopus 로고    scopus 로고
    • Preparation of coenzyme Q10 liposomes using supercritical anti-solvent technique
    • Xia, F., Jin, H., Zhao, Y., and Guo, X. (2012) Preparation of coenzyme Q10 liposomes using supercritical anti-solvent technique. J. Microencapsul. 29, 21-29.
    • (2012) J. Microencapsul. , vol.29 , pp. 21-29
    • Xia, F.1    Jin, H.2    Zhao, Y.3    Guo, X.4
  • 34
    • 77953625233 scopus 로고    scopus 로고
    • Curcumin nanoparticles improve the physicochemical properties of curcumin and effectively enhance its antioxidant and antihepatoma activities
    • Yen, F. L., Wu, T. H., Tzeng, C. W., Lin, L. T., and Lin, C. C. (2010) Curcumin nanoparticles improve the physicochemical properties of curcumin and effectively enhance its antioxidant and antihepatoma activities. J. Agric. Food Chem. 58, 7376-7382.
    • (2010) J Agric Food Chem , vol.58 , pp. 7376-7382
    • Yen, F.L.1    Wu, T.H.2    Tzeng, C.W.3    Lin, L.T.4    Lin, C.C.5
  • 35
    • 33644659990 scopus 로고    scopus 로고
    • Microencapsulation of α-tocopherol using sodium alginate and its controlled release properties
    • Yoo, S. H., Song, Y. B., Chang, P. S., and Lee, H. G. (2006) Microencapsulation of α-tocopherol using sodium alginate and its controlled release properties. Int. J. Biol. Macromol. 38, 25-30.
    • (2006) Int. J. Biol. Macromol. , vol.38 , pp. 25-30
    • Yoo, S.H.1    Song, Y.B.2    Chang, P.S.3    Lee, H.G.4
  • 36
    • 57749091590 scopus 로고    scopus 로고
    • Beta-lactoglobulin and its nanocomplexes with pectin as vehicles for ω-3 polyunsaturated fatty acids
    • Zimet, P. and Livney, Y. D. (2009) Beta-lactoglobulin and its nanocomplexes with pectin as vehicles for ω-3 polyunsaturated fatty acids. Food Hydrocolloid. 23, 1120-1126.
    • (2009) Food Hydrocolloid. , vol.23 , pp. 1120-1126
    • Zimet, P.1    Livney, Y.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.