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Volumn 25, Issue 5, 2011, Pages 1098-1104

Fabrication and characterization of TiO2/whey protein isolate nanocomposite film

Author keywords

Edible film; Self assembly; Titanium oxide; Whey protein isolate

Indexed keywords


EID: 79952533394     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2010.10.006     Document Type: Article
Times cited : (156)

References (34)
  • 4
    • 33745304184 scopus 로고    scopus 로고
    • Physics and chemistry of photocatalytic titanium dioxide: Visualization of bactericidal activity using atomic force microscopy
    • Banerjee S., Gopal J., Muraleedharan P., Tyagi A.K., Raj B. Physics and chemistry of photocatalytic titanium dioxide: Visualization of bactericidal activity using atomic force microscopy. Current Science 2006, 90(10):1378-1383.
    • (2006) Current Science , vol.90 , Issue.10 , pp. 1378-1383
    • Banerjee, S.1    Gopal, J.2    Muraleedharan, P.3    Tyagi, A.K.4    Raj, B.5
  • 5
    • 77955992292 scopus 로고    scopus 로고
    • Effects of the free and pre-encapsulated calcium ions on the physical properties of whey protein edible film
    • Chai Z., Shang J., Jiang Y., Ren F., Leng X. Effects of the free and pre-encapsulated calcium ions on the physical properties of whey protein edible film. International Journal of Food Science and Technology 2010, 45(7):1532-1538.
    • (2010) International Journal of Food Science and Technology , vol.45 , Issue.7 , pp. 1532-1538
    • Chai, Z.1    Shang, J.2    Jiang, Y.3    Ren, F.4    Leng, X.5
  • 7
    • 46949101060 scopus 로고    scopus 로고
    • Kinetics of the breakdown of cross-linked soy protein films for drug delivery
    • Chen L.Y., Remondetto G., Rouabhia M., Subirade M. Kinetics of the breakdown of cross-linked soy protein films for drug delivery. Biomaterials 2008, 29:3750-3756.
    • (2008) Biomaterials , vol.29 , pp. 3750-3756
    • Chen, L.Y.1    Remondetto, G.2    Rouabhia, M.3    Subirade, M.4
  • 9
    • 33750454055 scopus 로고    scopus 로고
    • Fourier transform Raman spectroscopy study of heat-induced gelation of plasma proteins as influenced by pH
    • Dàvila E., Parés D., Howell N.K. Fourier transform Raman spectroscopy study of heat-induced gelation of plasma proteins as influenced by pH. Journal of Agricultural and Food Chemistry 2006, 54:7890-7897.
    • (2006) Journal of Agricultural and Food Chemistry , vol.54 , pp. 7890-7897
    • Dàvila, E.1    Parés, D.2    Howell, N.K.3
  • 13
    • 15044348987 scopus 로고    scopus 로고
    • Utilization of front-face fluorescence spectroscopy for analysis of process cheese functionality
    • Garimella Purna S.K., Prow L.A., Metzger L.E. Utilization of front-face fluorescence spectroscopy for analysis of process cheese functionality. Journal of Dairy Science 2005, 88(2):470-477.
    • (2005) Journal of Dairy Science , vol.88 , Issue.2 , pp. 470-477
    • Garimella Purna, S.K.1    Prow, L.A.2    Metzger, L.E.3
  • 15
    • 77951260190 scopus 로고    scopus 로고
    • Study of the physical properties of whey protein isolate and gelatin composite films
    • Jiang Y., Li Y., Chai Z., Leng X. Study of the physical properties of whey protein isolate and gelatin composite films. Journal of Agricultural and Food Chemistry 2010, 58(8):5100-5108.
    • (2010) Journal of Agricultural and Food Chemistry , vol.58 , Issue.8 , pp. 5100-5108
    • Jiang, Y.1    Li, Y.2    Chai, Z.3    Leng, X.4
  • 16
    • 0036882032 scopus 로고    scopus 로고
    • Determination of lactulose and furosine in milk using front-face fluorescence spectroscopy
    • Kulmyrzaev A., Dufour É Determination of lactulose and furosine in milk using front-face fluorescence spectroscopy. Lait 2002, 82(6):725-735.
    • (2002) Lait , vol.82 , Issue.6 , pp. 725-735
    • Kulmyrzaev, A.1    Dufour É2
  • 17
    • 0015895751 scopus 로고
    • Quenching of protein fluorescence by oxygen: detection of structural fluctuations in proteins on the nanosecond time scale
    • Lakowicz J.R., Weber G. Quenching of protein fluorescence by oxygen: detection of structural fluctuations in proteins on the nanosecond time scale. Biochemistry 1973, 12(21):4171-4179.
    • (1973) Biochemistry , vol.12 , Issue.21 , pp. 4171-4179
    • Lakowicz, J.R.1    Weber, G.2
  • 18
    • 33744994533 scopus 로고    scopus 로고
    • A simple and direct isolation of whey components from raw milk by gel filtration chromatography and structural characterization by Fourier transform Raman spectroscopy
    • Liang M., Chen V.Y.T., Chen H.-L., Chen W.L. A simple and direct isolation of whey components from raw milk by gel filtration chromatography and structural characterization by Fourier transform Raman spectroscopy. Talanta 2006, 69(5):1269-1277.
    • (2006) Talanta , vol.69 , Issue.5 , pp. 1269-1277
    • Liang, M.1    Chen, V.Y.T.2    Chen, H.-L.3    Chen, W.L.4
  • 19
    • 0033833121 scopus 로고    scopus 로고
    • On the structure of particulate gels-the case of salt-induced cold gelation of heat-denatured whey protein isolate
    • Marangoni A.G., Barbut S., McGauley S.E., Marcone M., Narine S.S. On the structure of particulate gels-the case of salt-induced cold gelation of heat-denatured whey protein isolate. Food Hydrocolloids 2000, 14(1):61-74.
    • (2000) Food Hydrocolloids , vol.14 , Issue.1 , pp. 61-74
    • Marangoni, A.G.1    Barbut, S.2    McGauley, S.E.3    Marcone, M.4    Narine, S.S.5
  • 21
    • 17144428919 scopus 로고    scopus 로고
    • Fluorescence characteristics of several whey samples subjected to different treatments and conditions
    • Murillo Pulgarićn J.A., Molina A.A., Pardo M.T.A. Fluorescence characteristics of several whey samples subjected to different treatments and conditions. Analytica Chimica Acta 2005, 536(1-2):153-158.
    • (2005) Analytica Chimica Acta , vol.536 , Issue.1-2 , pp. 153-158
    • Murillo Pulgarićn, J.A.1    Molina, A.A.2    Pardo, M.T.A.3
  • 22
    • 6344277284 scopus 로고    scopus 로고
    • Comparison of changes in the secondary structure of unheated, heated, and high-pressure-treated β-lactoglobulin and ovalbumin proteins using Fourier transform Raman spectroscopy and self-deconvolution
    • Ngarize S., Herman H., Adams A., Howell N. Comparison of changes in the secondary structure of unheated, heated, and high-pressure-treated β-lactoglobulin and ovalbumin proteins using Fourier transform Raman spectroscopy and self-deconvolution. Journal of Agricultural and Food Chemistry 2004, 52:6470-6477.
    • (2004) Journal of Agricultural and Food Chemistry , vol.52 , pp. 6470-6477
    • Ngarize, S.1    Herman, H.2    Adams, A.3    Howell, N.4
  • 23
    • 0028104529 scopus 로고
    • Correlation between particle size, in vivo particle persistence, and lung injury
    • Oberdorster G., Ferin J., Lehnert B.E. Correlation between particle size, in vivo particle persistence, and lung injury. Environmental Health Perspectives 1994, 102(5):173-179.
    • (1994) Environmental Health Perspectives , vol.102 , Issue.5 , pp. 173-179
    • Oberdorster, G.1    Ferin, J.2    Lehnert, B.E.3
  • 24
  • 25
    • 47849084850 scopus 로고    scopus 로고
    • Formulation and stability of biodegradable films made from cod gelatin and sunflower oil blends
    • Pérez-Mateos M., Montero P., Gómez-Guillén M.C. Formulation and stability of biodegradable films made from cod gelatin and sunflower oil blends. Food Hydrocolloids 2009, 23:53-61.
    • (2009) Food Hydrocolloids , vol.23 , pp. 53-61
    • Pérez-Mateos, M.1    Montero, P.2    Gómez-Guillén, M.C.3
  • 26
    • 32244448003 scopus 로고    scopus 로고
    • Layer-by-layer fabrication and characterization of gold-nanoparticle/myoglobin nanocomposite films
    • Qi Z.M., Honma I., Ichihara M., Zhou H.S. Layer-by-layer fabrication and characterization of gold-nanoparticle/myoglobin nanocomposite films. Advanced Functional Materials 2006, 16(3):377-386.
    • (2006) Advanced Functional Materials , vol.16 , Issue.3 , pp. 377-386
    • Qi, Z.M.1    Honma, I.2    Ichihara, M.3    Zhou, H.S.4
  • 28
    • 76649093281 scopus 로고    scopus 로고
    • Advances in biomimetic and nanostructured biohybrid materials
    • Ruiz-Hitzky E., Darder M., Aranda P., Ariga K. Advances in biomimetic and nanostructured biohybrid materials. Advanced Materials 2010, 22(3):323-336.
    • (2010) Advanced Materials , vol.22 , Issue.3 , pp. 323-336
    • Ruiz-Hitzky, E.1    Darder, M.2    Aranda, P.3    Ariga, K.4
  • 30
    • 33644853479 scopus 로고    scopus 로고
    • Antimicrobial activity of whey protein based edible films incorporated with oregano, rosemary and garlic essential oils
    • Seydim A.C., Sarikus G. Antimicrobial activity of whey protein based edible films incorporated with oregano, rosemary and garlic essential oils. Food Research International 2006, 39(5):639-644.
    • (2006) Food Research International , vol.39 , Issue.5 , pp. 639-644
    • Seydim, A.C.1    Sarikus, G.2
  • 31
    • 38049174051 scopus 로고    scopus 로고
    • Preparation of composite film of soy protein and titania nanoparticles and its properties
    • Song X.-L., Zhou J.-H., Zhu C.-H., Ye J.-Y., Huang W. Preparation of composite film of soy protein and titania nanoparticles and its properties. Modern Chemical Industry 2007, 27:40-43.
    • (2007) Modern Chemical Industry , vol.27 , pp. 40-43
    • Song, X.-L.1    Zhou, J.-H.2    Zhu, C.-H.3    Ye, J.-Y.4    Huang, W.5
  • 33
    • 0025117123 scopus 로고
    • Tensile strength of discontinuous fibre-reinforced composites
    • Termonia Y. Tensile strength of discontinuous fibre-reinforced composites. Journal of Materials Science 1990, 25(11):4644-4653.
    • (1990) Journal of Materials Science , vol.25 , Issue.11 , pp. 4644-4653
    • Termonia, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.