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Volumn 45, Issue 1, 1997, Pages 23-29

Molecular Modifications of β-Lactoglobulin upon Exposure to High Pressure

Author keywords

High pressure treatments; Protein association; Protein structure; Lactoglobulin

Indexed keywords


EID: 0002739905     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf960330w     Document Type: Article
Times cited : (99)

References (43)
  • 1
    • 21344491096 scopus 로고
    • Effects of high pressure on proteins
    • Balny, C.; Masson, P. Effects of high pressure on proteins. Food Rev. Int. 1993, 9, 611-628.
    • (1993) Food Rev. Int. , vol.9 , pp. 611-628
    • Balny, C.1    Masson, P.2
  • 2
    • 84963456797 scopus 로고
    • Some recent aspects of the use of high-pressure for protein investigation in solution
    • Balny, C.; Masson, P.; Travers, F. Some recent aspects of the use of high-pressure for protein investigation in solution. High Pressure Res. 1989, 2, 1-28.
    • (1989) High Pressure Res. , vol.2 , pp. 1-28
    • Balny, C.1    Masson, P.2    Travers, F.3
  • 3
    • 0038276022 scopus 로고
    • Real-time monitoring of the surface hydrophobicity changes associated with isothermal treatment of milk and milk protein fractions
    • Bonomi, F.; Iametti, S. Real-time monitoring of the surface hydrophobicity changes associated with isothermal treatment of milk and milk protein fractions. Milchwissenschaft 1994, 46, 71-74.
    • (1994) Milchwissenschaft , vol.46 , pp. 71-74
    • Bonomi, F.1    Iametti, S.2
  • 4
    • 0028290324 scopus 로고
    • Reversible and irreversible modifications of β-lactoglobulin upon exposure to heat
    • Cairoli, S.; Iametti, S.; Bonomi, F. Reversible and irreversible modifications of β-lactoglobulin upon exposure to heat. J. Protein Chem. 1994, 13, 347-354.
    • (1994) J. Protein Chem. , vol.13 , pp. 347-354
    • Cairoli, S.1    Iametti, S.2    Bonomi, F.3
  • 5
    • 0000872633 scopus 로고
    • Effects of high pressure on food constituents
    • Balny, C., Hayashi, R., Heremans, K., Masson, P., Eds.; Colloques INSERM, John Libbey Eurotext: Montrouge, France
    • Cheftel, J. C. Effects of high pressure on food constituents. In High Pressure and Biotechnology; Balny, C., Hayashi, R., Heremans, K., Masson, P., Eds.; Colloques INSERM, John Libbey Eurotext: Montrouge, France, 1992; Vol. 224, pp 195-209.
    • (1992) High Pressure and Biotechnology , vol.224 , pp. 195-209
    • Cheftel, J.C.1
  • 6
    • 85007844131 scopus 로고
    • Effects of various heat treatments on structure and solubility of whey proteins
    • DeWit, J. N.; Klarenbeek, G. Effects of various heat treatments on structure and solubility of whey proteins. J. Dairy Sci. 1984, 67, 2701-2710.
    • (1984) J. Dairy Sci. , vol.67 , pp. 2701-2710
    • DeWit, J.N.1    Klarenbeek, G.2
  • 7
    • 0028180075 scopus 로고
    • High-pressure effects on β-lactoglobulin interactions with ligands studied by fluorescence
    • Dufour, E.; Hui Bon Hoa, G.; Haertle, T. High-pressure effects on β-lactoglobulin interactions with ligands studied by fluorescence. Biochim. Biophys. Acta 1994, 1206, 166-172.
    • (1994) Biochim. Biophys. Acta , vol.1206 , pp. 166-172
    • Dufour, E.1    Hui Bon Hoa, G.2    Haertle, T.3
  • 8
    • 0028950420 scopus 로고
    • Hydrolysis of β-lactoglobulin by thermolysin and trypsin under high hydrostatic pressure
    • Dufour, E.; Hervè, G.; Haertle, T. Hydrolysis of β-lactoglobulin by thermolysin and trypsin under high hydrostatic pressure. Biopolymers 1995, 35, 475-483.
    • (1995) Biopolymers , vol.35 , pp. 475-483
    • Dufour, E.1    Hervè, G.2    Haertle, T.3
  • 9
    • 0000521535 scopus 로고
    • High-pressure unfolding and aggregation of β-lactoglobulin and baroprotective effects of sucrose
    • Dumay, E.; Kalichevsky, M. T.; Cheftel, J. C. High-pressure unfolding and aggregation of β-lactoglobulin and baroprotective effects of sucrose. J. Agric. Food Chem. 1994, 42, 1861-1868.
    • (1994) J. Agric. Food Chem. , vol.42 , pp. 1861-1868
    • Dumay, E.1    Kalichevsky, M.T.2    Cheftel, J.C.3
  • 10
  • 11
    • 33751392636 scopus 로고
    • Surface hydrophobicity changes and heat-induced modifications of α-lactalbumin
    • Eynard, L.; Iametti, S.; Relkin, P.; Bonomi, F. Surface hydrophobicity changes and heat-induced modifications of α-lactalbumin. J. Agric. Food Chem. 1992, 40, 1731-1736.
    • (1992) J. Agric. Food Chem. , vol.40 , pp. 1731-1736
    • Eynard, L.1    Iametti, S.2    Relkin, P.3    Bonomi, F.4
  • 12
    • 0000940306 scopus 로고
    • Pressure-induced aggregation of β-lactoglobulin in pH 7.0 buffers
    • Funtenberg, S.; Dumay, E.; Cheftel, J. C. Pressure-induced aggregation of β-lactoglobulin in pH 7.0 buffers. Lebensm. Wiss. Technol. 1995, 28, 410-418.
    • (1995) Lebensm. Wiss. Technol. , vol.28 , pp. 410-418
    • Funtenberg, S.1    Dumay, E.2    Cheftel, J.C.3
  • 14
    • 0001341678 scopus 로고
    • β-Lactoglobulin
    • Fox, P. F., Ed.; Elsevier: London
    • Hambling, S. G.; McAlpine, A.; Sawyer, L. β-Lactoglobulin. In Milk Proteins; Fox, P. F., Ed.; Elsevier: London, 1992; pp 141-190.
    • (1992) Milk Proteins , pp. 141-190
    • Hambling, S.G.1    McAlpine, A.2    Sawyer, L.3
  • 15
    • 0001118101 scopus 로고
    • Utilization of pressure in addition to temperature in food science and technology
    • Balny, C., Hayashi, R., Heremans, K., Masson, P., Eds.; Colloques INSERM, John Libbey Eurotext: Montrouge, France
    • Hayashi, R. Utilization of pressure in addition to temperature in food science and technology. In High Pressure and Biotechnology; Balny, C., Hayashi, R., Heremans, K., Masson, P., Eds.; Colloques INSERM, John Libbey Eurotext: Montrouge, France, 1992; Vol. 224, pp 185-193.
    • (1992) High Pressure and Biotechnology , vol.224 , pp. 185-193
    • Hayashi, R.1
  • 16
    • 84987378217 scopus 로고
    • Introduction of high pressure to food processing: Preferential proteolysis of β-lactoglobulin in milk whey
    • Hayashi, R.; Kawamura, Y.; Kunugi, S. Introduction of high pressure to food processing: preferential proteolysis of β-lactoglobulin in milk whey. J. Food Sci. 1987, 52, 1107-1108.
    • (1987) J. Food Sci. , vol.52 , pp. 1107-1108
    • Hayashi, R.1    Kawamura, Y.2    Kunugi, S.3
  • 17
    • 0642302641 scopus 로고
    • Monitoring the surface hydrophobicity of milk proteins: A real-time study on heat-induced modifications
    • Iametti, S.; Bonomi, F. Monitoring the surface hydrophobicity of milk proteins: a real-time study on heat-induced modifications. Int. Dairy Fed. Bull. 1993, Special Issue No. 9303, 111-116.
    • (1993) Int. Dairy Fed. Bull. , Issue.9303 SPEC. ISSUE , pp. 111-116
    • Iametti, S.1    Bonomi, F.2
  • 18
    • 0002284922 scopus 로고
    • Modification of high-order structures upon heating of β-lactoglobulin: Dependence on the protein concentration
    • Iametti, S.; Cairoli, S.; De Gregori, B.; Bonomi, F. Modification of high-order structures upon heating of β-lactoglobulin: dependence on the protein concentration. J. Agric. Food Chem. 1995, 43, 53-58.
    • (1995) J. Agric. Food Chem. , vol.43 , pp. 53-58
    • Iametti, S.1    Cairoli, S.2    De Gregori, B.3    Bonomi, F.4
  • 19
    • 0029924648 scopus 로고    scopus 로고
    • Modifications at different structural levels occur during the heat denaturation of β-lactoglobulin
    • Iametti, S.; De Gregori, B.; Vecchio, G.; Bonomi, F. Modifications at different structural levels occur during the heat denaturation of β-lactoglobulin. Eur. J. Biochem 1996, 237, 106-112.
    • (1996) Eur. J. Biochem , vol.237 , pp. 106-112
    • Iametti, S.1    De Gregori, B.2    Vecchio, G.3    Bonomi, F.4
  • 20
    • 0026320508 scopus 로고
    • Protein stability and molecular adaptation to extreme conditions
    • Jaenicke, R. Protein stability and molecular adaptation to extreme conditions. Eur. J. Biochem. 1991, 202, 715-728.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 715-728
    • Jaenicke, R.1
  • 21
    • 0023669402 scopus 로고
    • Rapid formation of secondary structure framework in protein folding studied by stopped-flow circular dichroism
    • Kuwajima, K.; Yamaya, H.; Miwa, S.; Sugai, S.; Nagamura, T. Rapid formation of secondary structure framework in protein folding studied by stopped-flow circular dichroism. FEBS Lett. 1987, 221, 115-118.
    • (1987) FEBS Lett. , vol.221 , pp. 115-118
    • Kuwajima, K.1    Yamaya, H.2    Miwa, S.3    Sugai, S.4    Nagamura, T.5
  • 22
    • 0023661017 scopus 로고
    • Crystal structure of the trigonal form of bovine β-lactoglobulin and its complex with retinol at 2.5 Å resolution
    • Monaco, H. L.; Zanotti, G.; Spadon, P.; Bolognesi, M.; Sawyer, L.; Eliopoulos, E. E. Crystal structure of the trigonal form of bovine β-lactoglobulin and its complex with retinol at 2.5 Å resolution. J. Mol. Biol. 1987, 197, 695-706.
    • (1987) J. Mol. Biol. , vol.197 , pp. 695-706
    • Monaco, H.L.1    Zanotti, G.2    Spadon, P.3    Bolognesi, M.4    Sawyer, L.5    Eliopoulos, E.E.6
  • 23
    • 21144469137 scopus 로고
    • Production of low antigenic whey protein hydrolysates by enzymatic hydrolysis and denaturation with high pressure
    • Nakamura, T.; Sado, H.; Syukunobe, Y. Production of low antigenic whey protein hydrolysates by enzymatic hydrolysis and denaturation with high pressure. Milchwissenschaft 1993, 48, 141-145.
    • (1993) Milchwissenschaft , vol.48 , pp. 141-145
    • Nakamura, T.1    Sado, H.2    Syukunobe, Y.3
  • 24
    • 0002648948 scopus 로고
    • An analytical approach to the evaluation of heat damage in commercial milks
    • Pagliarini, E.; Iametti, S.; Peri, C.; Bonomi, F. An analytical approach to the evaluation of heat damage in commercial milks. J. Dairy Sci. 1990, 73, 41-44.
    • (1990) J. Dairy Sci. , vol.73 , pp. 41-44
    • Pagliarini, E.1    Iametti, S.2    Peri, C.3    Bonomi, F.4
  • 26
    • 0021876620 scopus 로고
    • Homology of β-lactoglobulin, serum retinol-binding protein and protein HC
    • Pervaiz, S.; Brew, K. Homology of β-lactoglobulin, serum retinol-binding protein and protein HC. Science 1985, 228, 335-337.
    • (1985) Science , vol.228 , pp. 335-337
    • Pervaiz, S.1    Brew, K.2
  • 27
    • 0000118732 scopus 로고    scopus 로고
    • The foaming properties of pressure treated β-casein
    • Pittia, P.; Wilde, P. J.; Clark, D. C. The foaming properties of pressure treated β-casein. Food Hydrocolloids 1996, 10, 335-342.
    • (1996) Food Hydrocolloids , vol.10 , pp. 335-342
    • Pittia, P.1    Wilde, P.J.2    Clark, D.C.3
  • 28
    • 0002940127 scopus 로고    scopus 로고
    • The molten globule state
    • Creighton, T. E., Ed.; Freeman: New York, 1992
    • Ptitsyn, O. B. The molten globule state. In Protein Folding; Creighton, T. E., Ed.; Freeman: New York, 1992; pp 243-300.
    • Protein Folding , pp. 243-300
    • Ptitsyn, O.B.1
  • 29
    • 0028567981 scopus 로고
    • A model for the denaturation and aggregation of β-lactoglobulin
    • Roefs, S. P. F. M.; De Kruif, K. G. A model for the denaturation and aggregation of β-lactoglobulin. Eur. J. Biochem. 1994, 226, 883-889.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 883-889
    • Roefs, S.P.F.M.1    De Kruif, K.G.2
  • 30
    • 0020436746 scopus 로고
    • Theoretical aspects of the direct titration of natural water and its information yield for trace metals speciation
    • Ruzic, I. Theoretical aspects of the direct titration of natural water and its information yield for trace metals speciation. Anal. Chim. Acta 1982, 140, 99-113.
    • (1982) Anal. Chim. Acta , vol.140 , pp. 99-113
    • Ruzic, I.1
  • 31
    • 0000326329 scopus 로고
    • Sulfhydryl group/disulfide bond interchange reactions during heat-induced gelation of whey protein isolate
    • Shimada, K.; Cheftel, J. C. Sulfhydryl group/disulfide bond interchange reactions during heat-induced gelation of whey protein isolate. J. Agric. Food. Chem. 1989, 37, 161-168.
    • (1989) J. Agric. Food. Chem. , vol.37 , pp. 161-168
    • Shimada, K.1    Cheftel, J.C.2
  • 34
    • 0030078033 scopus 로고    scopus 로고
    • Effect of high hydrostatic pressure on the enzymic hydrolysis of β-lactoglobulin B by trypsin, thermolysin and pepsin
    • Stapelfeldt, H.; Petersen, P. H.; Kristiansen, K. R.; Qvist, K. B.; Skibsted, L. H. Effect of high hydrostatic pressure on the enzymic hydrolysis of β-lactoglobulin B by trypsin, thermolysin and pepsin. J. Dairy Res. 1996, 63, 111-118.
    • (1996) J. Dairy Res. , vol.63 , pp. 111-118
    • Stapelfeldt, H.1    Petersen, P.H.2    Kristiansen, K.R.3    Qvist, K.B.4    Skibsted, L.H.5
  • 35
    • 0015997959 scopus 로고
    • Aromatic contribution to circular dichroism spectra of proteins
    • Strickland, E. H. Aromatic contribution to circular dichroism spectra of proteins. CRC Crit. Rev. Biochem. 1974, 2, 113-175.
    • (1974) CRC Crit. Rev. Biochem. , vol.2 , pp. 113-175
    • Strickland, E.H.1
  • 36
    • 0030058251 scopus 로고    scopus 로고
    • Effect of pressure on the deuterium exchange reaction of α-lactalbumin and of β-lactoglobulin
    • Tanaka, N.; Kunugi, S. Effect of pressure on the deuterium exchange reaction of α-lactalbumin and of β-lactoglobulin. Int. J. Biol. Macromol. 1996, 18, 33-39.
    • (1996) Int. J. Biol. Macromol. , vol.18 , pp. 33-39
    • Tanaka, N.1    Kunugi, S.2
  • 37
    • 0029936006 scopus 로고    scopus 로고
    • Modification of the single unpaired sulfhydryl group of β-lactoglobulin under high pressure and the role of intermolecular S-S exchange in the pressure denaturation
    • Tanaka, N.; Tsurui, Y.; Kobayashi, I.; Kunugi, S. Modification of the single unpaired sulfhydryl group of β-lactoglobulin under high pressure and the role of intermolecular S-S exchange in the pressure denaturation. Int. J. Biol. Macromol. 1996, 19, 63-68.
    • (1996) Int. J. Biol. Macromol. , vol.19 , pp. 63-68
    • Tanaka, N.1    Tsurui, Y.2    Kobayashi, I.3    Kunugi, S.4
  • 38
    • 0342325481 scopus 로고
    • Pressure inactivation of α-chymotrypsin
    • Taniguchi, Y.; Suzuki, K. Pressure inactivation of α-chymotrypsin. J. Phys. Chem. 1983, 87, 5185-5193.
    • (1983) J. Phys. Chem. , vol.87 , pp. 5185-5193
    • Taniguchi, Y.1    Suzuki, K.2
  • 39
    • 0028793284 scopus 로고
    • A comparative rheological study of heat and high pressure induced whey protein gels
    • Van Camp, J.; Huyghebaert, A. A comparative rheological study of heat and high pressure induced whey protein gels. Food Chem. 1995, 54, 357-364.
    • (1995) Food Chem. , vol.54 , pp. 357-364
    • Van Camp, J.1    Huyghebaert, A.2
  • 40
    • 0000552061 scopus 로고
    • Tryptic and chymotryptic hydrolysis of β-lactoglobulin A, B and AB at ambient and high pressure
    • Van Willige, R. W. G.; Fitzgerald, R. J. Tryptic and chymotryptic hydrolysis of β-lactoglobulin A, B and AB at ambient and high pressure. Milchwissenschaft 1995, 50, 183-186.
    • (1995) Milchwissenschaft , vol.50 , pp. 183-186
    • Van Willige, R.W.G.1    Fitzgerald, R.J.2
  • 41
    • 84974326036 scopus 로고
    • Heat-induced changes in sulphydryl and disulfide levels of β-lactoglobulin A and the formation of polymers
    • Watanabe, K.; Klostermeyer, H. Heat-induced changes in sulphydryl and disulfide levels of β-lactoglobulin A and the formation of polymers. J. Dairy Res. 1976, 43, 411-418.
    • (1976) J. Dairy Res. , vol.43 , pp. 411-418
    • Watanabe, K.1    Klostermeyer, H.2
  • 42
    • 0020712468 scopus 로고
    • The effect of high pressure upon proteins and other biomolecules
    • Weber, G.; Drickamer, M. G. The effect of high pressure upon proteins and other biomolecules. Q. Rev. Biophys. 1983, 16, 89-112.
    • (1983) Q. Rev. Biophys. , vol.16 , pp. 89-112
    • Weber, G.1    Drickamer, M.G.2
  • 43
    • 0015820466 scopus 로고
    • Pressure denaturation of metamyoglobin
    • Zipp, A.; Kautzmann, W. Pressure denaturation of metamyoglobin. Biochemistry 1973, 12, 4217-4228.
    • (1973) Biochemistry , vol.12 , pp. 4217-4228
    • Zipp, A.1    Kautzmann, W.2


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