메뉴 건너뛰기




Volumn 25, Issue 5, 2011, Pages 928-934

Physical properties of acid milk gels: Acidification rate significantly interacts with cross-linking and heat treatment of milk

Author keywords

Acidification rate; Gel stiffness; Microbial transglutaminase; Milk proteins; Syneresis

Indexed keywords


EID: 79952536682     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2010.09.003     Document Type: Article
Times cited : (54)

References (40)
  • 1
    • 7444238786 scopus 로고    scopus 로고
    • Bulletin 916, revised 2009, American Dairy Products Institute, Elmhurst, IL, USA, ADPI
    • ADPI Standards for grades of dry milk, including methods of analysis 2009, Bulletin 916, revised 2009, American Dairy Products Institute, Elmhurst, IL, USA.
    • (2009) Standards for grades of dry milk, including methods of analysis
  • 2
    • 57049122325 scopus 로고    scopus 로고
    • Effect of temperature and rate of acidification on rheological properties of skim milk gels
    • Anema S.G. Effect of temperature and rate of acidification on rheological properties of skim milk gels. Journal of Food Processing and Preservation 2008, 32:1016-1033.
    • (2008) Journal of Food Processing and Preservation , vol.32 , pp. 1016-1033
    • Anema, S.G.1
  • 3
    • 17444362230 scopus 로고    scopus 로고
    • Rheological properties of acid gels prepared from pressure- and transglutaminase-treated skim milk
    • Anema S.G., Lauber S., Lee S.K., Henle T., Klostermeyer H. Rheological properties of acid gels prepared from pressure- and transglutaminase-treated skim milk. Food Hydrocolloids 2005, 19:879-887.
    • (2005) Food Hydrocolloids , vol.19 , pp. 879-887
    • Anema, S.G.1    Lauber, S.2    Lee, S.K.3    Henle, T.4    Klostermeyer, H.5
  • 4
    • 34547768357 scopus 로고    scopus 로고
    • Influence of transglutaminase protein cross-linking on the rennet coagulation of casein
    • Bönisch M.P., Heidebach T.C., Kulozik U. Influence of transglutaminase protein cross-linking on the rennet coagulation of casein. Food Hydrocolloids 2008, 22:288-297.
    • (2008) Food Hydrocolloids , vol.22 , pp. 288-297
    • Bönisch, M.P.1    Heidebach, T.C.2    Kulozik, U.3
  • 5
    • 33645407623 scopus 로고    scopus 로고
    • Inactivation of an indigenous transglutaminase inhibitor in milk serum by means of UHT-treatment and membrane separation techniques
    • Bönisch M.P., Tolkach A., Kulozik U. Inactivation of an indigenous transglutaminase inhibitor in milk serum by means of UHT-treatment and membrane separation techniques. International Dairy Journal 2006, 16:669-678.
    • (2006) International Dairy Journal , vol.16 , pp. 669-678
    • Bönisch, M.P.1    Tolkach, A.2    Kulozik, U.3
  • 6
    • 30744434157 scopus 로고    scopus 로고
    • The effect of the glucono-δ-lactone/caseinate ratio on sodium caseinate gelation
    • Braga A.L.M., Menossi M., Cunha R.L. The effect of the glucono-δ-lactone/caseinate ratio on sodium caseinate gelation. International Dairy Journal 2006, 16:389-398.
    • (2006) International Dairy Journal , vol.16 , pp. 389-398
    • Braga, A.L.M.1    Menossi, M.2    Cunha, R.L.3
  • 7
    • 0000458372 scopus 로고
    • Effect of denaturation of beta-lactoglobulin on texture properties of set-style nonfat yogurt. 1. Syneresis
    • Dannenberg F., Kessler H.G. Effect of denaturation of beta-lactoglobulin on texture properties of set-style nonfat yogurt. 1. Syneresis. Milchwissenschaft 1988, 43:632-635.
    • (1988) Milchwissenschaft , vol.43 , pp. 632-635
    • Dannenberg, F.1    Kessler, H.G.2
  • 8
    • 0000458372 scopus 로고
    • Effect of denaturation of beta-lactoglobulin on texture properties of set-style nonfat yogurt. 2. Firmness and flow properties
    • Dannenberg F., Kessler H.G. Effect of denaturation of beta-lactoglobulin on texture properties of set-style nonfat yogurt. 2. Firmness and flow properties. Milchwissenschaft 1988, 43:700-704.
    • (1988) Milchwissenschaft , vol.43 , pp. 700-704
    • Dannenberg, F.1    Kessler, H.G.2
  • 10
    • 0000570313 scopus 로고    scopus 로고
    • Supra-aggregates of casein micelles as a prelude to coagulation
    • de Kruif C.G. Supra-aggregates of casein micelles as a prelude to coagulation. Journal of Dairy Science 1998, 81:3019-3028.
    • (1998) Journal of Dairy Science , vol.81 , pp. 3019-3028
    • de Kruif, C.G.1
  • 11
    • 21744448778 scopus 로고    scopus 로고
    • Transglutaminase: effect on rheological properties, microstructure and permeability of set style acid skim milk gel
    • Færgemand M., Qvist K.B. Transglutaminase: effect on rheological properties, microstructure and permeability of set style acid skim milk gel. Food Hydrocolloids 1997, 11:287-292.
    • (1997) Food Hydrocolloids , vol.11 , pp. 287-292
    • Færgemand, M.1    Qvist, K.B.2
  • 12
    • 0014011698 scopus 로고
    • Mechanism of action of guinea pig liver transglutaminase. I. Purification and properties of the enzyme; identification of a functional cysteine essential for activity
    • Folk J.E., Cole P.W. Mechanism of action of guinea pig liver transglutaminase. I. Purification and properties of the enzyme; identification of a functional cysteine essential for activity. Journal of Biological Chemistry 1966, 241:5518-5525.
    • (1966) Journal of Biological Chemistry , vol.241 , pp. 5518-5525
    • Folk, J.E.1    Cole, P.W.2
  • 14
    • 0032029213 scopus 로고    scopus 로고
    • Casein interactions: casting light on the black boxes, the structure in dairy products
    • Horne D.S. Casein interactions: casting light on the black boxes, the structure in dairy products. International Dairy Journal 1998, 8:171-177.
    • (1998) International Dairy Journal , vol.8 , pp. 171-177
    • Horne, D.S.1
  • 15
    • 0037433089 scopus 로고    scopus 로고
    • Casein micelles as hard spheres: limitations of the model in acidified gel formation
    • Horne D.S. Casein micelles as hard spheres: limitations of the model in acidified gel formation. Colloids and Surfaces A: Physicochemical and Engineering Aspects 2003, 213:255-263.
    • (2003) Colloids and Surfaces A: Physicochemical and Engineering Aspects , vol.213 , pp. 255-263
    • Horne, D.S.1
  • 16
    • 33845943546 scopus 로고    scopus 로고
    • Rennet-induced coagulation of enzymatically cross-linked casein micelles
    • Huppertz T., de Kruif C.G. Rennet-induced coagulation of enzymatically cross-linked casein micelles. International Dairy Journal 2007, 17:442-448.
    • (2007) International Dairy Journal , vol.17 , pp. 442-448
    • Huppertz, T.1    de Kruif, C.G.2
  • 17
    • 33845917620 scopus 로고    scopus 로고
    • Ethanol stability of casein micelles cross-linked with transglutaminase
    • Huppertz T., de Kruif C.G. Ethanol stability of casein micelles cross-linked with transglutaminase. International Dairy Journal 2007, 17:436-441.
    • (2007) International Dairy Journal , vol.17 , pp. 436-441
    • Huppertz, T.1    de Kruif, C.G.2
  • 21
    • 76749093576 scopus 로고    scopus 로고
    • Excessive cross-linking of caseins by microbial transglutaminase and its impact on physical properties of acidified milk gels
    • Jaros D., Jacob M., Otto C., Rohm H. Excessive cross-linking of caseins by microbial transglutaminase and its impact on physical properties of acidified milk gels. International Dairy Journal 2010, 20:341-347.
    • (2010) International Dairy Journal , vol.20 , pp. 341-347
    • Jaros, D.1    Jacob, M.2    Otto, C.3    Rohm, H.4
  • 22
    • 33645726443 scopus 로고    scopus 로고
    • Transglutaminase in dairy products: chemistry, physics and applications
    • Jaros D., Partschefeld C., Henle T., Rohm H. Transglutaminase in dairy products: chemistry, physics and 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
  • 23
    • 33748548082 scopus 로고    scopus 로고
    • Small and large deformation rheology of acid gels from transglutaminase treated milks
    • Jaros D., Pätzold J., Schwarzenbolz U., Rohm H. Small and large deformation rheology of acid gels from transglutaminase treated milks. Food Biophysics 2006, 1:124-132.
    • (2006) Food Biophysics , vol.1 , pp. 124-132
    • Jaros, D.1    Pätzold, J.2    Schwarzenbolz, U.3    Rohm, H.4
  • 24
    • 0035998505 scopus 로고    scopus 로고
    • Influence of the starter culture on the relationship between dry matter content and physical properties of set-style yogurt
    • Jaros D., Rohm H., Haque A., Bonaparte C., Kneifel W. Influence of the starter culture on the relationship between dry matter content and physical properties of set-style yogurt. Milchwissenschaft 2002, 57:325-328.
    • (2002) Milchwissenschaft , vol.57 , pp. 325-328
    • Jaros, D.1    Rohm, H.2    Haque, A.3    Bonaparte, C.4    Kneifel, W.5
  • 25
    • 0032382407 scopus 로고    scopus 로고
    • The effect of elevated milk solids and incubation temperature on the physical properties of natural yoghurt
    • Lankes H., Ozer H.B., Robinson R.K. The effect of elevated milk solids and incubation temperature on the physical properties of natural yoghurt. Milchwissenschaft 1998, 53:510-513.
    • (1998) Milchwissenschaft , vol.53 , pp. 510-513
    • Lankes, H.1    Ozer, H.B.2    Robinson, R.K.3
  • 26
    • 1642603877 scopus 로고    scopus 로고
    • Structure and physical properties of yogurt gels: effects of heating temperature and incubation temperature
    • Lee W.A., Lucey J.A. Structure and physical properties of yogurt gels: effects of heating temperature and incubation temperature. Journal of Texture Studies 2003, 34:515-536.
    • (2003) Journal of Texture Studies , vol.34 , pp. 515-536
    • Lee, W.A.1    Lucey, J.A.2
  • 27
    • 0036686486 scopus 로고    scopus 로고
    • Effect of enzymatic cross-linking of milk proteins on functional properties of set-style yoghurt
    • Lorenzen P.C., Neve H., Mautner A., Schlimme E. Effect of enzymatic cross-linking of milk proteins on functional properties of set-style yoghurt. International Journal of Dairy Technology 2002, 55:152-157.
    • (2002) International Journal of Dairy Technology , vol.55 , pp. 152-157
    • Lorenzen, P.C.1    Neve, H.2    Mautner, A.3    Schlimme, E.4
  • 28
    • 0031434231 scopus 로고    scopus 로고
    • Properties of acid casein gels made by acidification with glucono-δ-lactone. 2. Syneresis, permeability, and microstructural properties
    • Lucey J.A., van Vliet T., Grolle K., Geurts T., Walstra P. Properties of acid casein gels made by acidification with glucono-δ-lactone. 2. Syneresis, permeability, and microstructural properties. International Dairy Journal 1997, 7:389-397.
    • (1997) International Dairy Journal , vol.7 , pp. 389-397
    • Lucey, J.A.1    van Vliet, T.2    Grolle, K.3    Geurts, T.4    Walstra, P.5
  • 29
    • 70749103845 scopus 로고    scopus 로고
    • Microstructural changes in casein supramolecules during acidification of skim milk
    • McMahon D.J., Du H., McManus W.R., Larsen K.M. Microstructural changes in casein supramolecules during acidification of skim milk. Journal of Dairy Science 2009, 92:5854-5867.
    • (2009) Journal of Dairy Science , vol.92 , pp. 5854-5867
    • McMahon, D.J.1    Du, H.2    McManus, W.R.3    Larsen, K.M.4
  • 30
    • 44349125136 scopus 로고    scopus 로고
    • Supramolecular structure of the casein micelle
    • McMahon D.J., Oommen B.S. Supramolecular structure of the casein micelle. Journal of Dairy Science 2008, 91:1709-1721.
    • (2008) Journal of Dairy Science , vol.91 , pp. 1709-1721
    • McMahon, D.J.1    Oommen, B.S.2
  • 31
    • 0034247906 scopus 로고    scopus 로고
    • Structure and scaling behavior of aging rennet-induced casein gels examined by confocal microscopy and permeametry
    • Mellema M., Heesakkers J.W.M., van Opheusden J.H.J., van Vliet T. Structure and scaling behavior of aging rennet-induced casein gels examined by confocal microscopy and permeametry. Langmuir 2000, 16:6847-6854.
    • (2000) Langmuir , vol.16 , pp. 6847-6854
    • Mellema, M.1    Heesakkers, J.W.M.2    van Opheusden, J.H.J.3    van Vliet, T.4
  • 32
    • 25144525228 scopus 로고    scopus 로고
    • Influence of transglutaminase treatment on properties of micellar casein and products made therefrom
    • Mounsey J.S., O'Kennedy B.T., Kelly P.M. Influence of transglutaminase treatment on properties of micellar casein and products made therefrom. Lait 2005, 85:405-418.
    • (2005) Lait , vol.85 , pp. 405-418
    • Mounsey, J.S.1    O'Kennedy, B.T.2    Kelly, P.M.3
  • 33
    • 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
  • 34
    • 0036365981 scopus 로고    scopus 로고
    • Effect of transglutaminase on the heat stability of milk: a possible mechanism
    • O'Sullivan M.M., Kelly A.L., Fox P.F. Effect of transglutaminase on the heat stability of milk: a possible mechanism. Journal of Dairy Science 2002, 85:1-7.
    • (2002) Journal of Dairy Science , vol.85 , pp. 1-7
    • O'Sullivan, M.M.1    Kelly, A.L.2    Fox, P.F.3
  • 36
    • 24144467835 scopus 로고    scopus 로고
    • Physicochemical and structural characteristics of sodium caseinate biopolymers induced by microbial transglutaminase
    • Tang C., Yang X.Q., Chen Z., Wu H., Peng Z.Y. Physicochemical and structural characteristics of sodium caseinate biopolymers induced by microbial transglutaminase. Journal of Food Biochemistry 2005, 29:402-421.
    • (2005) Journal of Food Biochemistry , vol.29 , pp. 402-421
    • Tang, C.1    Yang, X.Q.2    Chen, Z.3    Wu, H.4    Peng, Z.Y.5
  • 37
    • 0007674510 scopus 로고    scopus 로고
    • Structure of whey protein gels, studied by permeability, scanning electron microscopy and rheology
    • Verheul M., Roefs S.P.F.M. Structure of whey protein gels, studied by permeability, scanning electron microscopy and rheology. Food Hydrocolloids 1998, 12:17-24.
    • (1998) Food Hydrocolloids , vol.12 , pp. 17-24
    • Verheul, M.1    Roefs, S.P.F.M.2
  • 38
    • 0345814889 scopus 로고    scopus 로고
    • Effect of temperature and acidification rate on the fractal dimension of acidified casein aggregates
    • Vétier N., Desobry-Banon S., Ould Eleya M.M., Hardy J. Effect of temperature and acidification rate on the fractal dimension of acidified casein aggregates. Journal of Dairy Science 1997, 80:3161-3166.
    • (1997) Journal of Dairy Science , vol.80 , pp. 3161-3166
    • Vétier, N.1    Desobry-Banon, S.2    Ould Eleya, M.M.3    Hardy, J.4
  • 40
    • 4444266641 scopus 로고    scopus 로고
    • Cooling effects on a model rennet casein gel system: part II. Permeability and microscopy
    • Zhong Q., Daubert C.R., Velev O.D. Cooling effects on a model rennet casein gel system: part II. Permeability and microscopy. Langmuir 2004, 20:7406-7411.
    • (2004) Langmuir , vol.20 , pp. 7406-7411
    • Zhong, Q.1    Daubert, C.R.2    Velev, O.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.