메뉴 건너뛰기




Volumn 12, Issue 4, 1998, Pages 393-400

Study of the inhibitory effect of hydrophobic fluorescent markers on the enzymic coagulation of bovine casein micelles: Action of TNS

Author keywords

[No Author keywords available]

Indexed keywords

AGGLOMERATION; BINDING ENERGY; CASEIN; COAGULATION; EMISSION SPECTROSCOPY; ENERGY TRANSFER; FLUORESCENCE; FLUORESCENCE SPECTROSCOPY; HYDROPHOBICITY; MICELLES; NAPHTHALENE;

EID: 0007846072     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0268-005X(98)00037-X     Document Type: Article
Times cited : (6)

References (30)
  • 2
    • 0023644737 scopus 로고
    • Kinetics of milk coagulation. I. The kinetics of kappa casein hydrolysis in the presence of enzyme deactivation
    • Carlson, A., Hill, C., & Olson, N. (1987a). Kinetics of milk coagulation. I. The kinetics of kappa casein hydrolysis in the presence of enzyme deactivation. Biotechnology and Bioengineering, 29, 582-589.
    • (1987) Biotechnology and Bioengineering , vol.29 , pp. 582-589
    • Carlson, A.1    Hill, C.2    Olson, N.3
  • 3
    • 0023644736 scopus 로고
    • Kinetics of milk coagulation. II. Kinetics of secondary phase: Micelle flocculation
    • Carlson, A., Hill, C., & Olson, N. (1987b). Kinetics of milk coagulation. II. Kinetics of secondary phase: Micelle flocculation. Biotechnology and Bioengineering, 29, 590-600.
    • (1987) Biotechnology and Bioengineering , vol.29 , pp. 590-600
    • Carlson, A.1    Hill, C.2    Olson, N.3
  • 4
    • 0001336544 scopus 로고
    • 1 and alcohol dehydrogenase fluorescence quenching by acrylamide
    • 1 and alcohol dehydrogenase fluorescence quenching by acrylamide. Journal of Chemical Education, 70, (5), 425-428.
    • (1993) Journal of Chemical Education , vol.70 , Issue.5 , pp. 425-428
    • Coutinho, A.1    Prieto, M.2
  • 5
    • 84974327486 scopus 로고
    • Proteolysis and aggregation of casein micelles treated with immobilized or soluble chymosin
    • Dalgleish, D. G. (1979). Proteolysis and aggregation of casein micelles treated with immobilized or soluble chymosin. Journal of Dairy Research, 46, 653-661.
    • (1979) Journal of Dairy Research , vol.46 , pp. 653-661
    • Dalgleish, D.G.1
  • 6
    • 84974379663 scopus 로고
    • Coagulation of renneted bovine casein micelles: Dependence on temperature, calcium ion concentration and ionic strength
    • Dalgleish, D. G. (1983). Coagulation of renneted bovine casein micelles: dependence on temperature, calcium ion concentration and ionic strength. Journal of Dairy Research, 50, 331-340.
    • (1983) Journal of Dairy Research , vol.50 , pp. 331-340
    • Dalgleish, D.G.1
  • 7
    • 0000264468 scopus 로고
    • Three-dimensional molecular modeling of bovine coagulation
    • Farrell Jr., H. M., Brown, E. M., & Kumosinski, T. F. (1993). Three-dimensional molecular modeling of bovine coagulation. Food Structure, 12, 235-250.
    • (1993) Food Structure , vol.12 , pp. 235-250
    • Farrell H.M., Jr.1    Brown, E.M.2    Kumosinski, T.F.3
  • 8
    • 0007800172 scopus 로고
    • Effect of monovalent cations on the kinetics of renneted milk coagulation
    • Gatti, C. A., & Pires, M. S. (1995). Effect of monovalent cations on the kinetics of renneted milk coagulation. Journal of Dairy Research, 62, 667-672.
    • (1995) Journal of Dairy Research , vol.62 , pp. 667-672
    • Gatti, C.A.1    Pires, M.S.2
  • 10
    • 0007757078 scopus 로고
    • Spectrofluorimetric study on surface hydrophobicity of bovine casein micelles in solution and during enzymic coagulation
    • Gatti, C. A., Risso, P. H., & Pires, M. S. (1995). Spectrofluorimetric study on surface hydrophobicity of bovine casein micelles in solution and during enzymic coagulation. Journal of Agricultural and Food Chemistry, 43, 2339-2344.
    • (1995) Journal of Agricultural and Food Chemistry , vol.43 , pp. 2339-2344
    • Gatti, C.A.1    Risso, P.H.2    Pires, M.S.3
  • 12
    • 84974318039 scopus 로고
    • Mode of binding of ionic materials to casein micelles
    • Green, M. (1982). Mode of binding of ionic materials to casein micelles. Journal of Dairy Research, 49, 99-105.
    • (1982) Journal of Dairy Research , vol.49 , pp. 99-105
    • Green, M.1
  • 13
    • 0022713639 scopus 로고
    • Steric stabilization and casein micelle stability
    • Horne, D. S. (1986). Steric stabilization and casein micelle stability. Journal of Colloidal Interface Science, 111, 250-260.
    • (1986) Journal of Colloidal Interface Science , vol.111 , pp. 250-260
    • Horne, D.S.1
  • 14
    • 0003417861 scopus 로고
    • Oxford, United States: Oxford University Press
    • Hunter, R. J. (1986). Foundations of colloid science, Vol. I, Oxford, United States: Oxford University Press.
    • (1986) Foundations of Colloid Science , vol.1
    • Hunter, R.J.1
  • 15
    • 0028366461 scopus 로고
    • An ultraviolet spectrophotometric method to determine milk protein content in alkaline medium
    • Kuaye, A. Y. (1994). An ultraviolet spectrophotometric method to determine milk protein content in alkaline medium. Food Chemistry, 49, 207-211.
    • (1994) Food Chemistry , vol.49 , pp. 207-211
    • Kuaye, A.Y.1
  • 16
    • 0027661562 scopus 로고
    • Three-dimensional molecular modeling of bovine caseins: A refined, energy-minimized κ-casein structure
    • Kumosinski, T. F., Brown, E. M., & Farrell Jr., H. M. (1993). Three-dimensional molecular modeling of bovine caseins: A refined, energy-minimized κ-casein structure. Journal of Dairy Science, 76, 2507-2520.
    • (1993) Journal of Dairy Science , vol.76 , pp. 2507-2520
    • Kumosinski, T.F.1    Brown, E.M.2    Farrell H.M., Jr.3
  • 18
    • 0027359841 scopus 로고
    • A simple fluorimetric method for the estimation of ligand binding parameters in ligand-enzyme complexes
    • Leskovac, V., Trivić, S., & Pantelić, M. (1993). A simple fluorimetric method for the estimation of ligand binding parameters in ligand-enzyme complexes. Analytical Biochemistry, 214, 431-434.
    • (1993) Analytical Biochemistry , vol.214 , pp. 431-434
    • Leskovac, V.1    Trivić, S.2    Pantelić, M.3
  • 19
    • 0025756205 scopus 로고
    • Fluorescent probes for measuring the binding constants and distances between the metal ions bound to Esccherichia coli glutamine synthetase
    • Lin, W.-Y., Eads, C. D., & Villafranca, J. J. (1991). Fluorescent probes for measuring the binding constants and distances between the metal ions bound to Esccherichia coli glutamine synthetase. Biochemistry, 30, 3421-3426.
    • (1991) Biochemistry , vol.30 , pp. 3421-3426
    • Lin, W.-Y.1    Eads, C.D.2    Villafranca, J.J.3
  • 20
    • 0023185083 scopus 로고
    • Myelin basic protein binds heme at specific site near the tryptophan residue
    • Morris, S. J., Bradley, D., Campagnoni, A. T., & Stoner, G. L. (1987). Myelin basic protein binds heme at specific site near the tryptophan residue. Biochemistry, 26, 2175-2182.
    • (1987) Biochemistry , vol.26 , pp. 2175-2182
    • Morris, S.J.1    Bradley, D.2    Campagnoni, A.T.3    Stoner, G.L.4
  • 21
    • 0023096760 scopus 로고
    • Comparison of comformations of κ-casein, para-κ-casein and glycomacropeptide
    • Ono, T., Yada, R., Yutani, K., & Nakai, S. (1987). Comparison of comformations of κ-casein, para-κ-casein and glycomacropeptide. Biochimica et Biophysica Acta, 911, 318-325.
    • (1987) Biochimica et Biophysica Acta , vol.911 , pp. 318-325
    • Ono, T.1    Yada, R.2    Yutani, K.3    Nakai, S.4
  • 22
    • 0000598705 scopus 로고
    • Stability and instability in disperse systems
    • Otewwill, R. H. (1977). Stability and instability in disperse systems. Journal of Colloid Interface Science, 58, 357-372.
    • (1977) Journal of Colloid Interface Science , vol.58 , pp. 357-372
    • Otewwill, R.H.1
  • 23
    • 0018461686 scopus 로고
    • Casein micelles: The colloid-chemical approach
    • Payens, T. (1979). Casein micelles: the colloid-chemical approach. Journal of Dairy Research, 46, 291-306.
    • (1979) Journal of Dairy Research , vol.46 , pp. 291-306
    • Payens, T.1
  • 24
    • 84974510129 scopus 로고
    • A study of surface hydrophobicity of milk proteins during enzymic coagulation and curd hardening
    • Peri, C., Pagliarini, E., Iametti, S., & Bonomi, F. (1990). A study of surface hydrophobicity of milk proteins during enzymic coagulation and curd hardening. Journal of Dairy Research, 57, 101-108.
    • (1990) Journal of Dairy Research , vol.57 , pp. 101-108
    • Peri, C.1    Pagliarini, E.2    Iametti, S.3    Bonomi, F.4
  • 25
    • 0017613512 scopus 로고
    • A simplication of the protein assay method of Lowry et al. which is more generally applicable
    • Peterson, G. L. (1977). A simplication of the protein assay method of Lowry et al. which is more generally applicable. Analytical Biochemistry, 83, 346-356.
    • (1977) Analytical Biochemistry , vol.83 , pp. 346-356
    • Peterson, G.L.1
  • 26
    • 33751028137 scopus 로고
    • Specificity and kenetics of the milk-clotting enzyme from Cardoon (Cynara cardunculus L.) toward bovine κ-casein
    • Queiroz Macedo, I., Faro, C. J., & Pires, E. M. (1993). Specificity and kenetics of the milk-clotting enzyme from Cardoon (Cynara cardunculus L.) toward bovine κ-casein. Journal of Agriculture and Food Chemistry, 41(10), 1537-1540.
    • (1993) Journal of Agriculture and Food Chemistry , vol.41 , Issue.10 , pp. 1537-1540
    • Queiroz MacEdo, I.1    Faro, C.J.2    Pires, E.M.3
  • 29
    • 85025797643 scopus 로고
    • On the stability of casein micelles
    • Walstra, P. (1990). On the stability of casein micelles. Journal of Dairy Science, 73, 1965-1979.
    • (1990) Journal of Dairy Science , vol.73 , pp. 1965-1979
    • Walstra, P.1
  • 30
    • 0015217218 scopus 로고
    • Fluorescent probes for conformational states of proteins. IV. The pepsinogen-pepsin conversion
    • Wang, J. L., & Edelman, G. M. (1971). Fluorescent probes for conformational states of proteins. IV. The pepsinogen-pepsin conversion Journal of Biological Chemistry, 246, 1185-1191.
    • (1971) Journal of Biological Chemistry , vol.246 , pp. 1185-1191
    • Wang, J.L.1    Edelman, G.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.