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Volumn 45, Issue 7, 1997, Pages 2514-2519

Cross-Linking of Milk Proteins with Transglutaminase at the Oil-Water Interface

Author keywords

Casein(ate); Enzymatic cross linking; Oil water interface; Protein film; Surface rheology; Surface shear viscosity; Transglutaminase; lactoglobulin

Indexed keywords


EID: 0642362759     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf9609789     Document Type: Article
Times cited : (82)

References (32)
  • 1
    • 0025377838 scopus 로고
    • Crosslinking of whey protein by transglutaminase
    • Aboumahmoud, R.; Savello, P. Crosslinking of whey protein by transglutaminase. J. Dairy Sci. 1990, 73, 256-263.
    • (1990) J. Dairy Sci. , vol.73 , pp. 256-263
    • Aboumahmoud, R.1    Savello, P.2
  • 2
    • 0342524367 scopus 로고
    • Surface behavior of adsorbed films of food proteins
    • Phillips, G. O., Wedlock, D. J., Williams, P. A., Eds.; Elsevier Applied Science: London
    • Castle, J.; Dickinson, E.; Murray, A.; Murray, B. S.; Stainsby, G. Surface behavior of adsorbed films of food proteins. In Gums and Stabilisers for the Food Industry 3; Phillips, G. O., Wedlock, D. J., Williams, P. A., Eds.; Elsevier Applied Science: London, 1986; pp 409-417.
    • (1986) Gums and Stabilisers for the Food Industry 3 , vol.3 , pp. 409-417
    • Castle, J.1    Dickinson, E.2    Murray, A.3    Murray, B.S.4    Stainsby, G.5
  • 3
    • 0000476470 scopus 로고
    • Interfacial interactions, competitive adsorption and emulsion stability
    • Chen, J.; Dickinson, E.; Iveson, G. Interfacial interactions, competitive adsorption and emulsion stability. Food Struct. 1993, 12, 135-146.
    • (1993) Food Struct. , vol.12 , pp. 135-146
    • Chen, J.1    Dickinson, E.2    Iveson, G.3
  • 4
    • 0025505415 scopus 로고
    • Effect of heat denaturation on the adsorption of β-lactoglobulin at the oil/water interface and on coalescence stability of emulsions
    • Das, K. P.; Kinsella, J. E. Effect of heat denaturation on the adsorption of β-lactoglobulin at the oil/water interface and on coalescence stability of emulsions. J. Colloid Interface Sci. 1990, 139, 551-560.
    • (1990) J. Colloid Interface Sci. , vol.139 , pp. 551-560
    • Das, K.P.1    Kinsella, J.E.2
  • 5
    • 84974122265 scopus 로고
    • Surface and emulsifying properties of caseins
    • Dickinson, E. Surface and emulsifying properties of caseins. J. Dairy Res. 1989, 56, 471-477.
    • (1989) J. Dairy Res. , vol.56 , pp. 471-477
    • Dickinson, E.1
  • 7
    • 0026026073 scopus 로고
    • Time-dependent polymerization of β-lactoglobulin through disulfide bonds at the oil-water interface in emulsions
    • Dickinson, E.; Matsumura, Y. Time-dependent polymerization of β-lactoglobulin through disulfide bonds at the oil-water interface in emulsions. Int. J. Biol. Macromol. 1991, 13, 26-30.
    • (1991) Int. J. Biol. Macromol. , vol.13 , pp. 26-30
    • Dickinson, E.1    Matsumura, Y.2
  • 8
    • 0001029829 scopus 로고
    • Surface coverage of β-lactoglobulin at the oil-water interface: Influence of protein heat treatment and various emulsifiers
    • Dickinson, E.; Hong, S.-T. Surface coverage of β-lactoglobulin at the oil-water interface: influence of protein heat treatment and various emulsifiers. J. Agric. Food Chem. 1994, 42, 1602-1606.
    • (1994) J. Agric. Food Chem. , vol.42 , pp. 1602-1606
    • Dickinson, E.1    Hong, S.-T.2
  • 9
    • 0028511883 scopus 로고
    • Proteins at liquid interfaces: Role of the molten globule state
    • Dickinson, E.; Matsumura, Y. Proteins at liquid interfaces: role of the molten globule state. Colloids Surf. B 1994, 3, 1-17.
    • (1994) Colloids Surf. B , vol.3 , pp. 1-17
    • Dickinson, E.1    Matsumura, Y.2
  • 10
    • 0000001743 scopus 로고    scopus 로고
    • Rheology of milk protein gels and protein-stabilized emulsion gels cross-linked with transglutaminase
    • Dickinson, E.; Yamamoto, Y. Rheology of milk protein gels and protein-stabilized emulsion gels cross-linked with transglutaminase. J. Agric. Food Chem. 1996, 44, 1371-1377.
    • (1996) J. Agric. Food Chem. , vol.44 , pp. 1371-1377
    • Dickinson, E.1    Yamamoto, Y.2
  • 11
    • 0022093211 scopus 로고
    • Time-dependent surface viscosity of adsorbed films of casein + gelatin at the oil-water interface
    • Dickinson, E.; Murray, B. S.; Stainsby, G. Time-dependent surface viscosity of adsorbed films of casein + gelatin at the oil-water interface. J. Colloid Interface Sci. 1985a, 106, 259-262.
    • (1985) J. Colloid Interface Sci. , vol.106 , pp. 259-262
    • Dickinson, E.1    Murray, B.S.2    Stainsby, G.3
  • 12
    • 0022059823 scopus 로고
    • Time-dependent surface pressures of adsorbed films of caseinate + gelatin at the oil-water interface
    • Dickinson, E.; Pogson, D. J.; Robson, E. W.; Stainsby, G. Time-dependent surface pressures of adsorbed films of caseinate + gelatin at the oil-water interface. Colloids Surf. 1985b, 14, 135-141.
    • (1985) Colloids Surf. , vol.14 , pp. 135-141
    • Dickinson, E.1    Pogson, D.J.2    Robson, E.W.3    Stainsby, G.4
  • 13
    • 0003790974 scopus 로고
    • Protein adsorption at air-water and oil-water interfaces
    • Dickinson, E., Stainsby, G., Eds.; Elsevier Applied Science: London
    • Dickinson, E.; Murray, B. S.; Stainsby, G. Protein adsorption at air-water and oil-water interfaces. In Advances in Food Emulsions and Foams; Dickinson, E., Stainsby, G., Eds.; Elsevier Applied Science: London, 1988a; pp 123-162.
    • (1988) Advances in Food Emulsions and Foams , pp. 123-162
    • Dickinson, E.1    Murray, B.S.2    Stainsby, G.3
  • 15
    • 0025007921 scopus 로고
    • Surface shear viscometry as a probe of protein-protein interactions in mixed milk protein films adsorbed at the oil-water interface
    • Dickinson, E.; Rolfe, S. E.; Dalgleish, D. G. Surface shear viscometry as a probe of protein-protein interactions in mixed milk protein films adsorbed at the oil-water interface. Int. J. Biol. Macromol. 1990, 12, 189-194.
    • (1990) Int. J. Biol. Macromol. , vol.12 , pp. 189-194
    • Dickinson, E.1    Rolfe, S.E.2    Dalgleish, D.G.3
  • 16
    • 37049090605 scopus 로고
    • Orthokinetic destabilization of a protein-stabilized emulsion by a water-soluble surfactant
    • Dickinson, E.; Owusu, R. K.; Williams, A. Orthokinetic destabilization of a protein-stabilized emulsion by a water-soluble surfactant. J. Chem. Soc., Faraday Trans. 1993, 89, 865-866.
    • (1993) J. Chem. Soc., Faraday Trans. , vol.89 , pp. 865-866
    • Dickinson, E.1    Owusu, R.K.2    Williams, A.3
  • 17
    • 85068945790 scopus 로고    scopus 로고
    • Unpublished results, Royal Veterinary and Agricultural University, Frederiksberg, Denmark
    • Færgemand, M., Unpublished results, Royal Veterinary and Agricultural University, Frederiksberg, Denmark, 1997.
    • (1997)
    • Færgemand, M.1
  • 18
    • 21744448778 scopus 로고    scopus 로고
    • Transglutaminase: Effect on rheological properties, microstructure and permeability of set style acid milk gel
    • in press
    • Færgemand, M.; Qvist, K. B. Transglutaminase: effect on rheological properties, microstructure and permeability of set style acid milk gel. Food Hydrocolloids 1997, in press.
    • (1997) Food Hydrocolloids
    • Færgemand, M.1    Qvist, K.B.2
  • 19
    • 21444433884 scopus 로고    scopus 로고
    • 2+ independent microbial transglutaminase from Streptomyces lydicus
    • 2+ independent microbial transglutaminase from Streptomyces lydicus. Food Hydrocolloids 1997, 11, 19-26.
    • (1997) Food Hydrocolloids , vol.11 , pp. 19-26
    • Færgemand, M.1    Otte, J.2    Qvist, K.B.3
  • 20
    • 0015777139 scopus 로고
    • Molecular and catalytic properties of transglutaminases
    • Folk, J. E.; Chung, S. I. Molecular and catalytic properties of transglutaminases. Adv. Enzymol. 1969, 38, 109-191.
    • (1969) Adv. Enzymol. , vol.38 , pp. 109-191
    • Folk, J.E.1    Chung, S.I.2
  • 21
    • 0017680149 scopus 로고
    • The ∈-(γ-glutamyl) lysine cross-link and the catalytic role of transglutaminase
    • Folk, J. E.; Finlayson, J. S. The ∈-(γ-glutamyl) lysine cross-link and the catalytic role of transglutaminase. Adv. Protein Chem. 1977, 31, 2-120.
    • (1977) Adv. Protein Chem. , vol.31 , pp. 2-120
    • Folk, J.E.1    Finlayson, J.S.2
  • 23
    • 84954936295 scopus 로고
    • Crosslinking of soybean 7S and 11S proteins by transglutaminase
    • Ikura, K.; Kometani, T.; Sasaki, R.; Chiba, H. Crosslinking of soybean 7S and 11S proteins by transglutaminase. Agric. Biol. Chem. 1980b, 44, 1979-1984.
    • (1980) Agric. Biol. Chem. , vol.44 , pp. 1979-1984
    • Ikura, K.1    Kometani, T.2    Sasaki, R.3    Chiba, H.4
  • 24
    • 0001522863 scopus 로고
    • Gelation and gel properties of soybean glycinin in a transglutaminase-catalysed system
    • Kang, I. J.; Matsumura, Y.; Ikura, K.; Motoki, M.; Sakamoto, H.; Mori, T. Gelation and gel properties of soybean glycinin in a transglutaminase-catalysed system. J. Agric. Food Chem. 1994, 42, 159-165.
    • (1994) J. Agric. Food Chem. , vol.42 , pp. 159-165
    • Kang, I.J.1    Matsumura, Y.2    Ikura, K.3    Motoki, M.4    Sakamoto, H.5    Mori, T.6
  • 25
    • 85025558300 scopus 로고
    • Filler effects of oil droplets on the viscoelastic properties of emulsion gels
    • Matsumura, Y.; Kang, H.-J.; Sakamoto, H.; Motoki, M.; Mori, T. Filler effects of oil droplets on the viscoelastic properties of emulsion gels. Food Hydrocolloids 1993, 7, 227-240.
    • (1993) Food Hydrocolloids , vol.7 , pp. 227-240
    • Matsumura, Y.1    Kang, H.-J.2    Sakamoto, H.3    Motoki, M.4    Mori, T.5
  • 26
    • 0030044861 scopus 로고    scopus 로고
    • Enhanced susceptibility to transglutaminase reaction of α-lactalbumin in the molten globule state
    • Matsumura, Y.; Chanyongvorakul, Y.; Rumazawa, Y.; Ohtsuka, T.; Mori, T. Enhanced susceptibility to transglutaminase reaction of α-lactalbumin in the molten globule state. Biochim. Biophys. Acta 1996, 1292, 69-76.
    • (1996) Biochim. Biophys. Acta , vol.1292 , pp. 69-76
    • Matsumura, Y.1    Chanyongvorakul, Y.2    Rumazawa, Y.3    Ohtsuka, T.4    Mori, T.5
  • 27
    • 0000036050 scopus 로고
    • Gelation of casein and soybean globulins by transglutaminase
    • Nio, N.; Motoki, M.; Takinami, R. Gelation of casein and soybean globulins by transglutaminase. Agric. Biol. Chem. 1985, 49, 2283-2286.
    • (1985) Agric. Biol. Chem. , vol.49 , pp. 2283-2286
    • Nio, N.1    Motoki, M.2    Takinami, R.3
  • 28
    • 84954938461 scopus 로고
    • Gelation mechanism of protein solution by transglutaminase
    • Nio, N.; Motoki, M.; Takinami, R. Gelation mechanism of protein solution by transglutaminase. Agric. Biol. Chem. 1986a, 50, 851-855.
    • (1986) Agric. Biol. Chem. , vol.50 , pp. 851-855
    • Nio, N.1    Motoki, M.2    Takinami, R.3
  • 29
    • 0001081018 scopus 로고
    • Gelation of protein emulsion by transglutaminase
    • Nio, N.; Motoki, M.; Takinami, R. Gelation of protein emulsion by transglutaminase. Agric. Biol. Chem. 1986b, 50, 1409-1412.
    • (1986) Agric. Biol. Chem. , vol.50 , pp. 1409-1412
    • Nio, N.1    Motoki, M.2    Takinami, R.3
  • 30
    • 0028139777 scopus 로고
    • Strength of protein gels prepared with microbial transglutaminase as related to reaction conditions
    • Sakamoto, H.; Rumazawa, Y.; Motoki, M. Strength of protein gels prepared with microbial transglutaminase as related to reaction conditions. J. Food Sci. 1994, 59, 866-871.
    • (1994) J. Food Sci. , vol.59 , pp. 866-871
    • Sakamoto, H.1    Rumazawa, Y.2    Motoki, M.3


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