메뉴 건너뛰기




Volumn 32, Issue 2, 2013, Pages 271-277

Interfacial cross-linking of β-casein changes the structure of the adsorbed layer

Author keywords

Cross linking; Interface; Rheology; Thickness; Casein

Indexed keywords

CASEIN; ELASTICITY; ENZYMES;

EID: 84874016803     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2013.01.009     Document Type: Article
Times cited : (31)

References (28)
  • 1
    • 0002281292 scopus 로고
    • Structural and mechanical properties of biopolymer gels
    • Clark A., Ross-Murphy S. Structural and mechanical properties of biopolymer gels. Advances in Polymer Science 1987, 83:57-192.
    • (1987) Advances in Polymer Science , vol.83 , pp. 57-192
    • Clark, A.1    Ross-Murphy, S.2
  • 2
    • 51049104790 scopus 로고    scopus 로고
    • Exceptional stability of food foams using class II hydrophobin HFBII
    • Cox A.R., Aldred D.L., Russell A.B. Exceptional stability of food foams using class II hydrophobin HFBII. Food Hydrocolloids 2009, 23:366-376.
    • (2009) Food Hydrocolloids , vol.23 , pp. 366-376
    • Cox, A.R.1    Aldred, D.L.2    Russell, A.B.3
  • 4
    • 0031259385 scopus 로고    scopus 로고
    • Enzymic crosslinking as a tool for food colloid rheology control and interfacial stabilization, a review
    • Dickinson E. Enzymic crosslinking as a tool for food colloid rheology control and interfacial stabilization, a review. Trends in Food Science & Technology 1997, 8:334-339.
    • (1997) Trends in Food Science & Technology , vol.8 , pp. 334-339
    • Dickinson, E.1
  • 6
    • 83455171950 scopus 로고    scopus 로고
    • Enzymatic cross-linking of β-lactoglobulin in solution and at air-water interface: structural constraints
    • Ercili-Cura D., Partanen R., Husband F., Ridout M., Macierzanka A., Lille M., et al. Enzymatic cross-linking of β-lactoglobulin in solution and at air-water interface: structural constraints. Food Hydrocolloids 2012, 28:1-9.
    • (2012) Food Hydrocolloids , vol.28 , pp. 1-9
    • Ercili-Cura, D.1    Partanen, R.2    Husband, F.3    Ridout, M.4    Macierzanka, A.5    Lille, M.6
  • 7
    • 0001102046 scopus 로고    scopus 로고
    • Interfacial dilatational properties of milk proteins cross-linked by transglutaminase
    • Faergemand M., Murray B.S. Interfacial dilatational properties of milk proteins cross-linked by transglutaminase. Journal of Agricultural and Food Chemistry 1998, 46:884-890.
    • (1998) Journal of Agricultural and Food Chemistry , vol.46 , pp. 884-890
    • Faergemand, M.1    Murray, B.S.2
  • 10
    • 0036384879 scopus 로고    scopus 로고
    • Functionality of Bacillus proteinase hydrolysates of sodium caseinate
    • Flanagan J., FitzGerald R.J. Functionality of Bacillus proteinase hydrolysates of sodium caseinate. International Dairy Journal 2002, 12:737-748.
    • (2002) International Dairy Journal , vol.12 , pp. 737-748
    • Flanagan, J.1    FitzGerald, R.J.2
  • 11
    • 0037214940 scopus 로고    scopus 로고
    • Functional properties of Bacillus proteinase hydrolysates of sodium caseinate incubated with transglutaminase pre- and post-hydrolysis
    • Flanagan J., FitzGerald R.J. Functional properties of Bacillus proteinase hydrolysates of sodium caseinate incubated with transglutaminase pre- and post-hydrolysis. International Dairy Journal 2003, 13:135-143.
    • (2003) International Dairy Journal , vol.13 , pp. 135-143
    • Flanagan, J.1    FitzGerald, R.J.2
  • 13
    • 78650676786 scopus 로고    scopus 로고
    • Effect of protein structural integrity on cross-linking by tyrosinase evidenced by multidimensional heteronuclear magnetic resonance spectroscopy
    • Hellman M., Mattinen M.L., Fu B., Buchert J., Permi P. Effect of protein structural integrity on cross-linking by tyrosinase evidenced by multidimensional heteronuclear magnetic resonance spectroscopy. Journal of Biotechnology 2011, 151:143-150.
    • (2011) Journal of Biotechnology , vol.151 , pp. 143-150
    • Hellman, M.1    Mattinen, M.L.2    Fu, B.3    Buchert, J.4    Permi, P.5
  • 14
    • 0031279972 scopus 로고    scopus 로고
    • A comparison of the functional and interfacial properties of β-casein and dephosphorylated β-casein
    • Husband F., Wilde P., Mackie A., Garrood M. A comparison of the functional and interfacial properties of β-casein and dephosphorylated β-casein. Journal of Colloid and Interface Science 1997, 195:77-85.
    • (1997) Journal of Colloid and Interface Science , vol.195 , pp. 77-85
    • Husband, F.1    Wilde, P.2    Mackie, A.3    Garrood, M.4
  • 15
    • 33645726443 scopus 로고    scopus 로고
    • Transglutaminase in dairy products: chemistry, physics, applications
    • Jaros D., Partschefeld C., Henle T., Rohm H. Transglutaminase in dairy products: chemistry, physics, applications. Journal of Texture Studies 2006, 37:113-155.
    • (2006) Journal of Texture Studies , vol.37 , pp. 113-155
    • Jaros, D.1    Partschefeld, C.2    Henle, T.3    Rohm, H.4
  • 16
    • 28444472469 scopus 로고    scopus 로고
    • Enzyme-aided modification of chicken-breast myofibril proteins: effect of laccase and transglutaminase on gelation and thermal stability
    • Lantto R., Puolanne E., Kalkkinen N., Buchert J., Autio K. Enzyme-aided modification of chicken-breast myofibril proteins: effect of laccase and transglutaminase on gelation and thermal stability. Journal of Agricultural and Food Chemistry 2005, 53:9231-9237.
    • (2005) Journal of Agricultural and Food Chemistry , vol.53 , pp. 9231-9237
    • Lantto, R.1    Puolanne, E.2    Kalkkinen, N.3    Buchert, J.4    Autio, K.5
  • 17
    • 84862562805 scopus 로고    scopus 로고
    • Transglutaminase catalyzed cross-linking of sodium caseinate improves oxidative stability of flaxseed oil emulsion
    • Ma H., Forssell P., Kylli P., Lampi A.-M., Buchert J., Boer H., et al. Transglutaminase catalyzed cross-linking of sodium caseinate improves oxidative stability of flaxseed oil emulsion. Journal of Agricultural and Food Chemistry 2012, 60:6223-6229.
    • (2012) Journal of Agricultural and Food Chemistry , vol.60 , pp. 6223-6229
    • Ma, H.1    Forssell, P.2    Kylli, P.3    Lampi, A.-M.4    Buchert, J.5    Boer, H.6
  • 18
  • 19
    • 84871333757 scopus 로고    scopus 로고
    • Enzymatically structured emulsions in simulated gastrointestinal environment: Impact on interfacial proteolysis and diffusion in intestinal mucus
    • Macierzanka A., Böttger F., Rigby N.M., Lille M., Poutanen K., Mills E.N.C., et al. Enzymatically structured emulsions in simulated gastrointestinal environment: Impact on interfacial proteolysis and diffusion in intestinal mucus. Langmuir 2012, 28:17349-17362.
    • (2012) Langmuir , vol.28 , pp. 17349-17362
    • Macierzanka, A.1    Böttger, F.2    Rigby, N.M.3    Lille, M.4    Poutanen, K.5    Mills, E.N.C.6
  • 22
    • 0032023294 scopus 로고    scopus 로고
    • Properties of b-casein at the air/water interface as supported by surface rheological measurements
    • Mellema M., Clark D.C., Husband F.A., Mackie A.R. Properties of b-casein at the air/water interface as supported by surface rheological measurements. Langmuir 1998, 14:1753-1758.
    • (1998) Langmuir , vol.14 , pp. 1753-1758
    • Mellema, M.1    Clark, D.C.2    Husband, F.A.3    Mackie, A.R.4
  • 23
    • 33947699947 scopus 로고    scopus 로고
    • Effect of transglutaminase on rheological properties and microstructure of chemically acidified sodium caseinate gels
    • Myllärinen P., Buchert J., Autio K. Effect of transglutaminase on rheological properties and microstructure of chemically acidified sodium caseinate gels. International Dairy Journal 2007, 17:800-807.
    • (2007) International Dairy Journal , vol.17 , pp. 800-807
    • Myllärinen, P.1    Buchert, J.2    Autio, K.3
  • 25
    • 27144456183 scopus 로고    scopus 로고
    • Cross linking and rheological characterization of adsorbed protein layers at the oil-water interface
    • Romoscanu A.I., Mezzenga R. Cross linking and rheological characterization of adsorbed protein layers at the oil-water interface. Langmuir 2005, 21:9689-9697.
    • (2005) Langmuir , vol.21 , pp. 9689-9697
    • Romoscanu, A.I.1    Mezzenga, R.2
  • 26
    • 0035209417 scopus 로고    scopus 로고
    • Influence of transglutaminase treatment of skim milk on the formation of ε-(γ-glutamyl)lysine and the susceptibility of individual proteins towards crosslinking
    • Sharma R., Lorenzen P.C., Qvist K.B. Influence of transglutaminase treatment of skim milk on the formation of ε-(γ-glutamyl)lysine and the susceptibility of individual proteins towards crosslinking. International Dairy Journal 2001, 11:785-793.
    • (2001) International Dairy Journal , vol.11 , pp. 785-793
    • Sharma, R.1    Lorenzen, P.C.2    Qvist, K.B.3
  • 27
    • 0036976630 scopus 로고    scopus 로고
    • Characteristics of oil-water emulsions stabilised by an industrial α-lactalbumin concentrate, cross-linked before and after emulsification, by a microbial transglutaminase
    • Sharma R., Zakora M., Qvist K.B. Characteristics of oil-water emulsions stabilised by an industrial α-lactalbumin concentrate, cross-linked before and after emulsification, by a microbial transglutaminase. Food Chemistry 2002, 79:493-500.
    • (2002) Food Chemistry , vol.79 , pp. 493-500
    • Sharma, R.1    Zakora, M.2    Qvist, K.B.3
  • 28
    • 78649320536 scopus 로고    scopus 로고
    • Real-time measurement of oxygen transport across an oil-water emulsion interface
    • Tikekar R.V., Johnson A., Nitin N. Real-time measurement of oxygen transport across an oil-water emulsion interface. Journal of Food Engineering 2011, 103:14-20.
    • (2011) Journal of Food Engineering , vol.103 , pp. 14-20
    • Tikekar, R.V.1    Johnson, A.2    Nitin, N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.