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Volumn 64, Issue 3, 1999, Pages 396-399

Interactive effects of pressure, temperature and time on the molecular structure of β-lactoglobulin

Author keywords

Circular dichroism; High pressure; Tertiary structure; lactoglobulin

Indexed keywords


EID: 0032990151     PISSN: 00221147     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2621.1999.tb15050.x     Document Type: Article
Times cited : (18)

References (10)
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    • Box, G.E.P.1    Wilson, K.B.2
  • 2
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    • Influence of alcohol-containing spreading solvents on the secondary structure of proteins: A circular dichroism investigation
    • Clark, D. and Smith, L. 1989. Influence of alcohol-containing spreading solvents on the secondary structure of proteins: a circular dichroism investigation. Journal of Agric. Food Chem. 37: 627-633.
    • (1989) Journal of Agric. Food Chem. , vol.37 , pp. 627-633
    • Clark, D.1    Smith, L.2
  • 3
    • 84987322003 scopus 로고
    • Denaturation of bovine serum albumin (BSA) and ovalbumin by high hydrostatic pressure, heat and chemicals
    • Hayakawa, I., Kajuhara, J., Murikawa, K., Oda, M., and Fujio, Y. 1992. Denaturation of bovine serum albumin (BSA) and ovalbumin by high hydrostatic pressure, heat and chemicals J. Food Science 57: 288-292.
    • (1992) J. Food Science , vol.57 , pp. 288-292
    • Hayakawa, I.1    Kajuhara, J.2    Murikawa, K.3    Oda, M.4    Fujio, Y.5
  • 5
    • 0000302885 scopus 로고
    • Engineering aspects of high pressure technology in the food industry
    • Mertens, B. and Deplace, G. 1993. Engineering aspects of high pressure technology in the food industry. Food Technol. 47(6): 164-169.
    • (1993) Food Technol. , vol.47 , Issue.6 , pp. 164-169
    • Mertens, B.1    Deplace, G.2
  • 6
    • 0028650679 scopus 로고
    • Exploiting the effects of high hydrostatic pressure in biotechnological applications
    • Mozhaev, V., Heremans, K., Frank, J., Masson, P., and Balny, C. 1994. Exploiting the effects of high hydrostatic pressure in biotechnological applications. TIBTECH. 12: 493-501.
    • (1994) TIBTECH. , vol.12 , pp. 493-501
    • Mozhaev, V.1    Heremans, K.2    Frank, J.3    Masson, P.4    Balny, C.5
  • 7
    • 0030457343 scopus 로고    scopus 로고
    • Functional and structural properties of β-lactoglobulin as affected by high-pressure treatment
    • Pittia, P., Wilde, P., Husband, F., and Clark, D. 1996. Functional and structural properties of β-lactoglobulin as affected by high-pressure treatment. J. Food Sci. 61: 1123-1128.
    • (1996) J. Food Sci. , vol.61 , pp. 1123-1128
    • Pittia, P.1    Wilde, P.2    Husband, F.3    Clark, D.4
  • 8
    • 0000262049 scopus 로고
    • Circular dichroism in protein analysis: A comprehensive desk review
    • R.A. Meyers (Ed.). VCH, New York
    • Price, N.C. 1995. Circular dichroism in protein analysis: A comprehensive desk review. Mol. Biol. Biotech. R.A. Meyers (Ed.), p. 179-185. VCH, New York.
    • (1995) Mol. Biol. Biotech. , pp. 179-185
    • Price, N.C.1
  • 9
    • 0027762355 scopus 로고
    • Pressure stability of proteins
    • Silva, J. and Weber, G. 1993. Pressure stability of proteins. Ann. Rev. Phys. Chem. 44: 89-113.
    • (1993) Ann. Rev. Phys. Chem. , vol.44 , pp. 89-113
    • Silva, J.1    Weber, G.2
  • 10
    • 0032093977 scopus 로고    scopus 로고
    • Combined effects of thermal and pressure processing on food protein structure
    • Tedford, L-.A., Kelly, S.M., Price, N.C., and Schaschke, C.J. 1998. Combined effects of thermal and pressure processing on food protein structure. Trans. IChemE 76 (Part C): 80-86.
    • (1998) Trans. IChemE , vol.76 , Issue.PART C , pp. 80-86
    • Tedford, L.-A.1    Kelly, S.M.2    Price, N.C.3    Schaschke, C.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.