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Volumn 61, Issue 2, 1998, Pages

Irreversible high pressure inactivation of β-galactosidase from Kluyveromyces lactis: Comparison with thermal inactivation

Author keywords

galactosidase from Kluyveromyces lactis; Pressure; Stability; Temperature

Indexed keywords

ATMOSPHERIC PRESSURE; CATALYST DEACTIVATION; HIGH PRESSURE EFFECTS; HYDROSTATIC PRESSURE; IONIC STRENGTH; PHOSPHATES; RATE CONSTANTS; THERMAL EFFECTS;

EID: 0032522099     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-1656(98)00007-8     Document Type: Article
Times cited : (12)

References (37)
  • 1
    • 21344491096 scopus 로고
    • Effects of high pressure on proteins
    • Balny C., Masson P. Effects of high pressure on proteins. Food Rev. Int. 9:1993;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 investigations in solution
    • Balny C., Masson P., Travers F. Some recent aspects of the use of high-pressure for protein investigations in solution. High Press. Res. 2:1989;1-28.
    • (1989) High Press. Res. , vol.2 , pp. 1-28
    • Balny, C.1    Masson, P.2    Travers, F.3
  • 4
    • 0028982189 scopus 로고
    • Characterization of β-galactosidase from Kluyveromyces lactis
    • Cavaille D., Combes D. Characterization of β-galactosidase from Kluyveromyces lactis. Biotechnol. Appl. Biochem. 22:1995;55-64.
    • (1995) Biotechnol. Appl. Biochem. , vol.22 , pp. 55-64
    • Cavaille, D.1    Combes, D.2
  • 5
    • 0028848430 scopus 로고
    • Effect of temperature and pressure on yeast invertase stability: A kinetic and conformational study
    • Cavaille D., Combes D. Effect of temperature and pressure on yeast invertase stability: a kinetic and conformational study. J. Biotechnol. 43:1995;221-228.
    • (1995) J. Biotechnol. , vol.43 , pp. 221-228
    • Cavaille, D.1    Combes, D.2
  • 6
    • 0000601034 scopus 로고
    • Applications des hautes pressions en technologie alimentaire
    • Cheftel J.C. Applications des hautes pressions en technologie alimentaire. I.A.A. 108:1991;141-153.
    • (1991) I.A.A. , vol.108 , pp. 141-153
    • Cheftel, J.C.1
  • 7
    • 0000872633 scopus 로고
    • Effects of high hydrostatic pressure on food constituents: an overview
    • In: Balny, C., Hayashi, R., Heremans, K., Masson, P. (Eds.), J. Libbey, London, pp.
    • Cheftel, J.C., 1992. Effects of high hydrostatic pressure on food constituents: an overview. In: Balny, C., Hayashi, R., Heremans, K., Masson, P. (Eds.), High Pressure and Biotechnology, Colloque INSERM, vol. 224. J. Libbey, London, pp. 195-209.
    • (1992) High Pressure and Biotechnology, Colloque INSERM , vol.224 , pp. 195-209
    • Cheftel, J.C.1
  • 9
    • 0030029012 scopus 로고
    • Pressure-induced inactivation of E. Coli β-galactosidase: influence of pH and temperature
    • Degraeve, P., Delorme, P., Lemay, P., 1995. Pressure-induced inactivation of E. Coli β-galactosidase: influence of pH and temperature. Biochim. Biophys. Acta 1292, 61-68.
    • (1995) Biochim. Biophys. Acta , vol.1292 , pp. 61-68
    • Degraeve, P.1    Delorme, P.2    Lemay, P.3
  • 10
    • 0018341922 scopus 로고
    • Purification and properties of an inducible β-galactosidase isolated from the yeast Kluyveromyces lactis
    • Dickson R.C., Dickson L.R., Markin J.S. Purification and properties of an inducible β-galactosidase isolated from the yeast Kluyveromyces lactis. J. Bacteriol. 137:1979;51-61.
    • (1979) J. Bacteriol. , vol.137 , pp. 51-61
    • Dickson, R.C.1    Dickson, L.R.2    Markin, J.S.3
  • 11
    • 0030529382 scopus 로고    scopus 로고
    • Effect of monvalent cations on the stability of and activity of Kluyveromyces lactis β-galactosidase
    • Flores, M.V., Ertola, R.J., Voget, C.E., 1996. Effect of monvalent cations on the stability of and activity of Kluyveromyces lactis β-galactosidase. Lebensm. Wiss. U. Technol 29, 503-506.
    • (1996) Lebensm. Wiss. U. Technol , vol.29 , pp. 503-506
    • Flores, M.V.1    Ertola, R.J.2    Voget, C.E.3
  • 14
    • 0028220701 scopus 로고
    • Proteins under pressure: The influence of high hydrostatic pressure on structure, function and assembly of proteins and protein complexes
    • Gross M., Jaenicke R. Proteins under pressure: the influence of high hydrostatic pressure on structure, function and assembly of proteins and protein complexes. Eur. J. Biochem. 221:1994;617-630.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 617-630
    • Gross, M.1    Jaenicke, R.2
  • 15
    • 0015236387 scopus 로고
    • Reversible pressure-temperature denaturation of chymotrypsinogen
    • Hawley S.A. Reversible pressure-temperature denaturation of chymotrypsinogen. Biochemistry. 10:1971;2436-2442.
    • (1971) Biochemistry , vol.10 , pp. 2436-2442
    • Hawley, S.A.1
  • 16
    • 0016769552 scopus 로고
    • An electrophoretic study of reversible protein denaturation: Chymotrypsinogen at high pressures
    • Hawley S.A., Mitchell R.M. An electrophoretic study of reversible protein denaturation: chymotrypsinogen at high pressures. Biochemistry. 14:1975;3257-3264.
    • (1975) Biochemistry , vol.14 , pp. 3257-3264
    • Hawley, S.A.1    Mitchell, R.M.2
  • 17
    • 0001084601 scopus 로고
    • Advances in high pressure food processing technology in Japan
    • In: Gaonkar, A.G. (Ed.), Elsevier, Amsterdam, pp. - 195
    • Hayashi, R., 1995. Advances in high pressure food processing technology in Japan. In: Gaonkar, A.G. (Ed.), Food Processing: Recent Developments. Elsevier, Amsterdam, pp. 185 - 195.
    • (1995) Food Processing: Recent Developments , pp. 185
    • Hayashi, R.1
  • 18
    • 0028217082 scopus 로고
    • Pressure stabilization of proteins from extreme thermophiles
    • Hei D.J., Clark D.S. Pressure stabilization of proteins from extreme thermophiles. Appl. Environ. Microbiol. 60:1994;932-939.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 932-939
    • Hei, D.J.1    Clark, D.S.2
  • 19
    • 0022013872 scopus 로고
    • Categorization of enzyme inactivations using a series-type mechanism
    • Henley J.P., Sadana A. Categorization of enzyme inactivations using a series-type mechanism. Enzyme Microb. Technol. 7:1985;50-60.
    • (1985) Enzyme Microb. Technol. , vol.7 , pp. 50-60
    • Henley, J.P.1    Sadana, A.2
  • 20
    • 0020017199 scopus 로고
    • High pressure effects on proteins and other biomolecules
    • Heremans K. High pressure effects on proteins and other biomolecules. Annu. Rev. Biophys. Bioeng. 11:1982;1-21.
    • (1982) Annu. Rev. Biophys. Bioeng. , vol.11 , pp. 1-21
    • Heremans, K.1
  • 21
    • 0001057371 scopus 로고
    • Pressure effects on the Raman spectra of proteins: Pressure-induced changes in the conformation of lysozyme in aqueous solutions
    • Heremans K., Wong P.T.T. Pressure effects on the Raman spectra of proteins: pressure-induced changes in the conformation of lysozyme in aqueous solutions. Chem. Phys. Lett. 18:1985;101-104.
    • (1985) Chem. Phys. Lett. , vol.18 , pp. 101-104
    • Heremans, K.1    Wong, P.T.T.2
  • 22
    • 0028827595 scopus 로고
    • Enhanced thermotolerance by hydrostatic pressure in deap-sea hyperthermophile Pyrococcus strain ES4
    • Holden J.F., Baross J.A. Enhanced thermotolerance by hydrostatic pressure in deap-sea hyperthermophile Pyrococcus strain ES4. FEMS Microbiol. Ecol. 18:1995;27-34.
    • (1995) FEMS Microbiol. Ecol. , vol.18 , pp. 27-34
    • Holden, J.F.1    Baross, J.A.2
  • 23
    • 0027073244 scopus 로고
    • Enzyme reactions under high pressure and their applications
    • Kunugi S. Enzyme reactions under high pressure and their applications. Ann. New York Acad. Sci. 672:1992;293-304.
    • (1992) Ann. New York Acad. Sci. , vol.672 , pp. 293-304
    • Kunugi, S.1
  • 24
    • 0017054059 scopus 로고
    • Plurality of pressure-denatured forms in chymotrypsinogen and lysozyme
    • Li T.M., Hook III J.W., Drickamer H.G., Weber G. Plurality of pressure-denatured forms in chymotrypsinogen and lysozyme. Biochemistry. 15:1976;5571-5580.
    • (1976) Biochemistry , vol.15 , pp. 5571-5580
    • Li, T.M.1    Hook J.W. III2    Drickamer, H.G.3    Weber, G.4
  • 26
    • 0001110974 scopus 로고
    • Pressure effects on structure and activity of cholinesterase
    • In: Quinn, D.M. (Ed.), Plenum, New York, pp.
    • Masson, P., Clery, C., 1995. Pressure effects on structure and activity of cholinesterase. In: Quinn, D.M. (Ed.), Enzymes of the Cholinesterase Family. Plenum, New York, pp. 113-121.
    • (1995) Enzymes of the Cholinesterase Family , pp. 113-121
    • Masson, P.1    Clery, C.2
  • 27
    • 0028650679 scopus 로고
    • Exploiting the effects of high hydrostatic pressure in biotechnological applications
    • Mozhaev V.V., Heremans K., Frank J., Masson P., Balny C. Exploiting the effects of high hydrostatic pressure in biotechnological applications. TIBTECH. 12:1994;493-501.
    • (1994) TIBTECH , vol.12 , pp. 493-501
    • Mozhaev, V.V.1    Heremans, K.2    Frank, J.3    Masson, P.4    Balny, C.5
  • 29
    • 0028812197 scopus 로고
    • Sensitivity of vegetative pathogens to high hydrostatic pressure treatment in phosphate-buffered saline and foods
    • Patterson M.F., Quinn M., Simpson R., Gilmour A. Sensitivity of vegetative pathogens to high hydrostatic pressure treatment in phosphate-buffered saline and foods. J. Food Protect. 58:1995;524-529.
    • (1995) J. Food Protect. , vol.58 , pp. 524-529
    • Patterson, M.F.1    Quinn, M.2    Simpson, R.3    Gilmour, A.4
  • 30
    • 0028933961 scopus 로고
    • Les bactéries des fonds marins
    • Prieur, D., 1995. Les bactéries des fonds marins. Biofutur Mars, 24-26.
    • (1995) Biofutur Mars , pp. 24-26
    • Prieur, D.1
  • 33
    • 0029204505 scopus 로고
    • Pasteurization of food by hydrostatic high pressure: Chemical aspects
    • Tauscher B. Pasteurization of food by hydrostatic high pressure: chemical aspects. Z Lebens. Unters. Forsch. 200:1995;3-13.
    • (1995) Z Lebens. Unters. Forsch. , vol.200 , pp. 3-13
    • Tauscher, B.1
  • 35
    • 0000256164 scopus 로고
    • Dynamics of oligomeric proteins
    • Weber G. Dynamics of oligomeric proteins. J. Mol. Liq. 42:1989;255-268.
    • (1989) J. Mol. Liq. , vol.42 , pp. 255-268
    • Weber, G.1
  • 37
    • 0023727267 scopus 로고
    • Pressure effects on protein secondary structure and hydrogen deuterium exchange in chymotrypsinogen: A Fourier transform infrared spectroscopic study
    • Wong P.T.T., Heremans K. Pressure effects on protein secondary structure and hydrogen deuterium exchange in chymotrypsinogen: a Fourier transform infrared spectroscopic study. Biochim. Biophys. Acta. 956:1988;1-9.
    • (1988) Biochim. Biophys. Acta , vol.956 , pp. 1-9
    • Wong, P.T.T.1    Heremans, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.