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Volumn 16, Issue 2, 2002, Pages 95-103

Stability parameters for β-lactoglobulin thermal dissociation and unfolding in phosphate buffer at pH 7.0

Author keywords

Beta lactoglobulin; Denaturation; Heat Stability; Stability function relations; Unfolding

Indexed keywords

DENATURATION; DIMERS; FREE ENERGY; GIBBS FREE ENERGY; MONOMERS; THERMODYNAMIC STABILITY;

EID: 0036149249     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0268-005X(01)00067-4     Document Type: Article
Times cited : (33)

References (46)
  • 31
    • 0026564078 scopus 로고
    • The effect of calcium on bovine α-lactalbumin conformational transitions by ultraviolet and fluorescence spectrophotometry
    • (1992) Food Chemistry , vol.43 , pp. 41-45
    • Owusu, R.K.1
  • 37
    • 85025552328 scopus 로고
    • Concentration effects on the kinetics of beta-lactoglobulin heat denaturation: A differential scanning calorimetric study
    • (1990) Food Hydrocolloids , vol.4 , pp. 19-32
    • Relkin, P.1    Launay, B.2
  • 39
    • 0003071279 scopus 로고
    • Glass transition-related physicochemical changes in foods
    • (1995) Food Technology , vol.49 , Issue.10 , pp. 97-102
    • Roos, Y.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.