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Volumn 52, Issue 14, 2004, Pages 4465-4471

Heat-induced changes in the ultrasonic properties of whey proteins

Author keywords

Ultrasound spectroscopy; Whey protein gelation

Indexed keywords

ALPHA LACTALBUMIN; BETA LACTOGLOBULIN; UNCLASSIFIED DRUG; VEGETABLE PROTEIN; WHEY PROTEIN;

EID: 3142655323     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf0354390     Document Type: Article
Times cited : (33)

References (25)
  • 1
    • 85025567869 scopus 로고
    • Fine-stranded and particulate gels of β-lactoglobulin and whey proteins at varying pH
    • Langton, M.; Hermansson, A. M. Fine-stranded and particulate gels of β-lactoglobulin and whey proteins at varying pH. Food Hydrocolloids 1992, 5, 523-539.
    • (1992) Food Hydrocolloids , vol.5 , pp. 523-539
    • Langton, M.1    Hermansson, A.M.2
  • 2
    • 0000083806 scopus 로고    scopus 로고
    • Rheological study on the fractal nature of the protein gel structure
    • Ikeda, S.; Foegeding, E. A.; Hagiwara, T. Rheological study on the fractal nature of the protein gel structure. Langmuir 1999, 15, 8584-8589.
    • (1999) Langmuir , vol.15 , pp. 8584-8589
    • Ikeda, S.1    Foegeding, E.A.2    Hagiwara, T.3
  • 3
    • 0036704306 scopus 로고    scopus 로고
    • Recent advances in the characterization of heat-induced aggregates and intermediates of whey proteins
    • De la Fuente, M. A.; Singh, H.; Hemar, Y. Recent advances in the characterization of heat-induced aggregates and intermediates of whey proteins. Trends Food Sci. Technol. 2002, 13, 262-274.
    • (2002) Trends Food Sci. Technol. , vol.13 , pp. 262-274
    • De La Fuente, M.A.1    Singh, H.2    Hemar, Y.3
  • 4
    • 0029924648 scopus 로고    scopus 로고
    • Modifications occur at different structural levels during the heat denaturation of β-lactoglobulin
    • Iametti, S.; De Gregori, B.; Vecchio, G.; Bonomi, F. Modifications occur at different structural levels 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
  • 5
    • 0001245634 scopus 로고
    • NMR studies of thermal denaturation and cation-mediated aggregation of β-lactoglobulin
    • Li, H.; Harding, C. C.; Foegeding, E. A. NMR studies of thermal denaturation and cation-mediated aggregation of β-lactoglobulin. J. Agric. Food Chem. 1994, 42, 2411-2420.
    • (1994) J. Agric. Food Chem. , vol.42 , pp. 2411-2420
    • Li, H.1    Harding, C.C.2    Foegeding, E.A.3
  • 6
    • 0001230130 scopus 로고
    • Differential scanning calorimetry: A useful tool for studying protein denaturation
    • Relkin, P. Differential scanning calorimetry: a useful tool for studying protein denaturation. Thermochim. Acta 1994, 246, 371-386.
    • (1994) Thermochim. Acta , vol.246 , pp. 371-386
    • Relkin, P.1
  • 7
    • 0001029710 scopus 로고    scopus 로고
    • Growth and structures of aggregates of heat denatured β-lactoglobulin
    • Le bon, C.; Nicolai, T.; Durand, D. Growth and structures of aggregates of heat denatured β-lactoglobulin. Int. J. Food Sci. Technol. 1999, 31, 451-466.
    • (1999) Int. J. Food Sci. Technol. , vol.31 , pp. 451-466
    • Le Bon, C.1    Nicolai, T.2    Durand, D.3
  • 8
    • 0036196674 scopus 로고    scopus 로고
    • Fine stranded and particulate aggregates of heat-denatured whey proteins visualized by atomic force microscopy
    • Ikeda, S.; Morris, V. J. Fine stranded and particulate aggregates of heat-denatured whey proteins visualized by atomic force microscopy. Biomacromolecules 2002, 3, 382-389.
    • (2002) Biomacromolecules , vol.3 , pp. 382-389
    • Ikeda, S.1    Morris, V.J.2
  • 9
    • 0001266819 scopus 로고    scopus 로고
    • Molecular mass distributions of heat-induced β-lactoglobulin aggregates
    • Hoffmann, M. A. M.; Sala, G.; Olieman, C.; de Kruif, K. G. Molecular mass distributions of heat-induced β-lactoglobulin aggregates. J. Agric. Food Chem. 1997, 45, 2949-2957.
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 2949-2957
    • Hoffmann, M.A.M.1    Sala, G.2    Olieman, C.3    De Kruif, K.G.4
  • 10
    • 0033501546 scopus 로고    scopus 로고
    • Characterization of intermediates formed during heat-induced aggregation of β-lactoglobulin AB at neutral pH
    • Schokker, E. P.; Sing, H.; Pinder, D. N.; Norris, G. E.; Creamer, L. K. Characterization of intermediates formed during heat-induced aggregation of β-lactoglobulin AB at neutral pH. Int. Dairy J. 1999, 9, 791-800.
    • (1999) Int. Dairy J. , vol.9 , pp. 791-800
    • Schokker, E.P.1    Sing, H.2    Pinder, D.N.3    Norris, G.E.4    Creamer, L.K.5
  • 11
    • 0001406422 scopus 로고    scopus 로고
    • Interactions between α-lactalbumin and β-lactoglobulin in the early stages of heat denaturation
    • Dalgleish, D. G.; Senaratne, V.; Francois, S. Interactions between α-lactalbumin and β-lactoglobulin in the early stages of heat denaturation. J. Agric. Food Chem. 1997, 45, 3459-3464.
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 3459-3464
    • Dalgleish, D.G.1    Senaratne, V.2    Francois, S.3
  • 12
    • 0034462997 scopus 로고    scopus 로고
    • Heat-induced aggregation of β-lactoglobulin A and B with α-lactalbumin
    • Schokker, E. P.; Singh, A. M.; Creamer, L. K. Heat-induced aggregation of β-lactoglobulin A and B with α-lactalbumin. Int. Dairy J. 2000, 10, 843-853.
    • (2000) Int. Dairy J. , vol.10 , pp. 843-853
    • Schokker, E.P.1    Singh, A.M.2    Creamer, L.K.3
  • 13
    • 0039136058 scopus 로고    scopus 로고
    • Ultrasonic spectrometry study of the influence of temperature on whey protein aggregation
    • Bryant, C. M.; McClements, D. J. Ultrasonic spectrometry study of the influence of temperature on whey protein aggregation. Food Hydrocolloids 1999, 13, 439-444.
    • (1999) Food Hydrocolloids , vol.13 , pp. 439-444
    • Bryant, C.M.1    McClements, D.J.2
  • 14
    • 0015513454 scopus 로고
    • Ultrasonic absorption mechanisms in aqueous solutions of bovine haemoglobin
    • O'Brien, W. D.; Dunn, F. Ultrasonic absorption mechanisms in aqueous solutions of bovine haemoglobin. J. Phys. Chem. 1972, 76, 528-533.
    • (1972) J. Phys. Chem. , vol.76 , pp. 528-533
    • O'Brien, W.D.1    Dunn, F.2
  • 15
    • 0034435173 scopus 로고    scopus 로고
    • Ultrasonic high-resolution longitudinal and shear wave measurements in food colloids: Monitoring of gelation processes and detection of pathogens
    • Kudryashov, E.; Smyth, C.; Duffy, G.; Buckin, V. Ultrasonic high-resolution longitudinal and shear wave measurements in food colloids: monitoring of gelation processes and detection of pathogens. Prog. Colloid Polym. Sci. 2000, 115, 287-294.
    • (2000) Prog. Colloid Polym. Sci. , vol.115 , pp. 287-294
    • Kudryashov, E.1    Smyth, C.2    Duffy, G.3    Buckin, V.4
  • 16
    • 2642536783 scopus 로고    scopus 로고
    • Studies of the acid gelation of milk using ultrasonic spectroscopy and diffusing wave spectroscopy
    • in press
    • Dalgleish, D. G.; Alexander, M.; Corredig, M. Studies of the acid gelation of milk using ultrasonic spectroscopy and diffusing wave spectroscopy. Food Hydrocolloids 2004, in press.
    • (2004) Food Hydrocolloids
    • Dalgleish, D.G.1    Alexander, M.2    Corredig, M.3
  • 17
    • 0022402481 scopus 로고
    • Rapid analysis of bovine milk proteins by fast protein liquid chromatography
    • Andrews, A. T.; Taylor, M. D.; Owen, A. J. Rapid analysis of bovine milk proteins by fast protein liquid chromatography. J. Chromatogr. 1985, 348, 177-185.
    • (1985) J. Chromatogr. , vol.348 , pp. 177-185
    • Andrews, A.T.1    Taylor, M.D.2    Owen, A.J.3
  • 18
    • 0001374270 scopus 로고    scopus 로고
    • High-resolution ultrasonic resonator measurements for analysis of liquids
    • Buckin, V.; Smyth, C. High-resolution ultrasonic resonator measurements for analysis of liquids. Sem. Food Anal. 1999, 4, 113-130.
    • (1999) Sem. Food Anal. , vol.4 , pp. 113-130
    • Buckin, V.1    Smyth, C.2
  • 19
    • 0002696861 scopus 로고
    • Hydration of nucleic bases in dilute aqueous solutions. Apparent molar volumes and their temperature slopes at 25 °C
    • Buckin, V. A. Hydration of nucleic bases in dilute aqueous solutions. Apparent molar volumes and their temperature slopes at 25 °C. Biophys. Chem. 1988, 29, 283-292.
    • (1988) Biophys. Chem. , vol.29 , pp. 283-292
    • Buckin, V.A.1
  • 20
    • 33845561444 scopus 로고
    • Compressibility of globular proteins in water at 25 °C
    • Gekko, K.; Noguchi, H. Compressibility of globular proteins in water at 25 °C. J. Phys. Chem. 1979, 83, 2706-2714.
    • (1979) J. Phys. Chem. , vol.83 , pp. 2706-2714
    • Gekko, K.1    Noguchi, H.2
  • 21
    • 0040056165 scopus 로고    scopus 로고
    • The suitability of scanning calorimetry to investigate slow irreversible protein denaturation
    • Hoffmann, M. A. M.; van Miltenburg, J. C.; van Mil, P. J. J. M. The suitability of scanning calorimetry to investigate slow irreversible protein denaturation. Thermochim. Acta 1997, 306, 45-49.
    • (1997) Thermochim. Acta , vol.306 , pp. 45-49
    • Hoffmann, M.A.M.1    Van Miltenburg, J.C.2    Van Mil, P.J.J.M.3
  • 22
    • 0001744217 scopus 로고    scopus 로고
    • Use of differential scanning calorimetry and infrared spectroscopy in the study of thermal and structural stability of α-lactalbumin
    • Boye, J. I.; Alli, I.; Ismail, A. A. Use of differential scanning calorimetry and infrared spectroscopy in the study of thermal and structural stability of α-lactalbumin. J. Agric. Food Chem. 1997, 45, 1116-1125.
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 1116-1125
    • Boye, J.I.1    Alli, I.2    Ismail, A.A.3
  • 24
    • 0038746782 scopus 로고    scopus 로고
    • Cold-set globular protein gels: Interactions, structure and rheology as a function of protein concentration
    • Alting, A. C.; Hamer, R. J.; de Kruif, C. G.; Visschers, R. W. Cold-set globular protein gels: interactions, structure and rheology as a function of protein concentration. J. Agric. Food Chem. 2003, 51, 3150-3156.
    • (2003) J. Agric. Food Chem. , vol.51 , pp. 3150-3156
    • Alting, A.C.1    Hamer, R.J.2    De Kruif, C.G.3    Visschers, R.W.4
  • 25
    • 0342467949 scopus 로고    scopus 로고
    • Heat-induced gelation of whey protein isolate (WPI): Effect of NaCl and protein concentration
    • Puyol, P.; Perez, M. D.; Horne, D. S. Heat-induced gelation of whey protein isolate (WPI): effect of NaCl and protein concentration. Food Hydrocolloids 2001, 15, 233-237.
    • (2001) Food Hydrocolloids , vol.15 , pp. 233-237
    • Puyol, P.1    Perez, M.D.2    Horne, D.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.