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Volumn 105, Issue 3, 2003, Pages 235-243

Experimental modelling of thermal inactivation of urease

Author keywords

Experimental modelling; Flow calorimetry; Inactivation mechanism and kinetics; Jack bean urease; Thermal inactivation

Indexed keywords

ASSOCIATION REACTIONS; CALORIMETRY; DISSOCIATION; ENTHALPY; ENZYMES; PH EFFECTS; PHOSPHATES;

EID: 0142214495     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2003.07.005     Document Type: Article
Times cited : (42)

References (19)
  • 1
    • 0029043937 scopus 로고
    • Enzyme immobilization on an epoxy matrix. Determination of L-arginine by flow-injection techniques
    • Alonso A., Almendral M.J., Baez M.D., Porras M.J., Alonso C. Enzyme immobilization on an epoxy matrix. Determination of L-arginine by flow-injection techniques. Anal. Chim. Acta. 308:1995;164-169.
    • (1995) Anal. Chim. Acta , vol.308 , pp. 164-169
    • Alonso, A.1    Almendral, M.J.2    Baez, M.D.3    Porras, M.J.4    Alonso, C.5
  • 2
    • 0034005332 scopus 로고    scopus 로고
    • A poly(n-sopropylacrylamide-co-N-acroloxysuccinimide-co-2-hydroxyetyl methacrylate) composite hydrogel membrane for urease immobilization to enhance urea hydrolysis rate by temperature swing
    • Chen J.P., Chiu S.H. A poly(n-sopropylacrylamide-co-N- acroloxysuccinimide-co-2-hydroxyetyl methacrylate) composite hydrogel membrane for urease immobilization to enhance urea hydrolysis rate by temperature swing. Enzyme Microb. Technol. 26:2000;359-367.
    • (2000) Enzyme Microb. Technol. , vol.26 , pp. 359-367
    • Chen, J.P.1    Chiu, S.H.2
  • 3
    • 0025231736 scopus 로고
    • Multi-analyte miniature conductance biosensor
    • Cullen D.C., Sethi R.S., Lowe C.R. Multi-analyte miniature conductance biosensor. Anal. Chim. Acta. 231:1990;33-40.
    • (1990) Anal. Chim. Acta , vol.231 , pp. 33-40
    • Cullen, D.C.1    Sethi, R.S.2    Lowe, C.R.3
  • 4
    • 0016846997 scopus 로고
    • Jack bean urease (EC3.5.1.5). A metalloenzyme. A simple biological role for nickel
    • Dixon N.E., Gazzola C., Blakeley R.L., Zerner B. Jack bean urease (EC3.5.1.5). A metalloenzyme. A simple biological role for nickel. J. Am. Chem. Soc. 97:1975;4131-4133.
    • (1975) J. Am. Chem. Soc. , vol.97 , pp. 4131-4133
    • Dixon, N.E.1    Gazzola, C.2    Blakeley, R.L.3    Zerner, B.4
  • 5
    • 0343632394 scopus 로고    scopus 로고
    • Immobilization of urease onto membranes of modified acrylonitrile copolymer
    • Godjevargova T., Dimov A. Immobilization of urease onto membranes of modified acrylonitrile copolymer. J. Membr. Sci. 135:1997;93-98.
    • (1997) J. Membr. Sci. , vol.135 , pp. 93-98
    • Godjevargova, T.1    Dimov, A.2
  • 6
    • 0027202218 scopus 로고
    • Structural-change of jack bean urease induced by addition of surfactants studied with synchrotron-radiation small-angle X-ray-scattering
    • Hirai M., Kawai-Hiral R., Hirai T. Structural-change of jack bean urease induced by addition of surfactants studied with synchrotron-radiation small-angle X-ray-scattering. Eur. J. Biochem. 215:1993;55-61.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 55-61
    • Hirai, M.1    Kawai-Hiral, R.2    Hirai, T.3
  • 7
    • 0026970477 scopus 로고
    • Effect of subunit dissociation, denaturation, aggregation, coagulation, and decomposition on enzyme inactivation kinetics. II. Biphasic and grace period behavior
    • Lencki W.R., Arul J., Neufeld R.J. Effect of subunit dissociation, denaturation, aggregation, coagulation, and decomposition on enzyme inactivation kinetics. II. Biphasic and grace period behavior. Biotechnol. Bioeng. 40:1992;1427-1434.
    • (1992) Biotechnol. Bioeng. , vol.40 , pp. 1427-1434
    • Lencki, W.R.1    Arul, J.2    Neufeld, R.J.3
  • 10
    • 0028964682 scopus 로고
    • Dissociation and unfolding of jack bean urease studied by fluorescence emission spectroscopy
    • Omar S., Beauregard M. Dissociation and unfolding of jack bean urease studied by fluorescence emission spectroscopy. J. Biotechnol. 39:1995;221-228.
    • (1995) J. Biotechnol. , vol.39 , pp. 221-228
    • Omar, S.1    Beauregard, M.2
  • 11
    • 0037010713 scopus 로고    scopus 로고
    • Modelling of the kinetics of thermal inactivation of glucoamylase from Aspergillus niger
    • Polakovič M., Bryjak J. Modelling of the kinetics of thermal inactivation of glucoamylase from Aspergillus niger. J. Mol. Catal. B. 19/20:2002;443-450.
    • (2002) J. Mol. Catal. B , vol.19 , Issue.20 , pp. 443-450
    • Polakovič, M.1    Bryjak, J.2
  • 12
    • 0030295092 scopus 로고    scopus 로고
    • Analysis of the mechanism and kinetics of thermal inactivation of enzymes: Critical assessment of isothermal inactivation experiments
    • Polakovič M., Vrábel P. Analysis of the mechanism and kinetics of thermal inactivation of enzymes: critical assessment of isothermal inactivation experiments. Process Biochem. 31:1996;787-800.
    • (1996) Process Biochem. , vol.31 , pp. 787-800
    • Polakovič, M.1    Vrábel, P.2
  • 13
    • 0036184268 scopus 로고    scopus 로고
    • Properties and applications of urease
    • Quin Y., Cabral J.M. Properties and applications of urease. Biocatal. Biotransform. 20:2002;227-236.
    • (2002) Biocatal. Biotransform. , vol.20 , pp. 227-236
    • Quin, Y.1    Cabral, J.M.2
  • 14
    • 0032472347 scopus 로고    scopus 로고
    • Preparation and characterization of urease bound on crosslinked poly(vinyl alcohol)
    • Rejikumar S., Devi S. Preparation and characterization of urease bound on crosslinked poly(vinyl alcohol). J. Mol. Catal. B. 4:1998;61-66.
    • (1998) J. Mol. Catal. B , vol.4 , pp. 61-66
    • Rejikumar, S.1    Devi, S.2
  • 15
    • 0028048961 scopus 로고
    • Development of an optical fibre sensor for ammonia, urea, urease and IgG
    • Sansubrino A., Mascini M. Development of an optical fibre sensor for ammonia, urea, urease and IgG. Biosens. Bioelectron. 9:1994;207-216.
    • (1994) Biosens. Bioelectron. , vol.9 , pp. 207-216
    • Sansubrino, A.1    Mascini, M.2
  • 16
    • 0033478810 scopus 로고    scopus 로고
    • Monitoring of soluble enzyme activity by enzyme flow microcalorimetry
    • Štefuca V., Polakovič M. Monitoring of soluble enzyme activity by enzyme flow microcalorimetry. Chem. Pap. 53:1999;362-365.
    • (1999) Chem. Pap. , vol.53 , pp. 362-365
    • Štefuca, V.1    Polakovič, M.2
  • 18
    • 0342683812 scopus 로고    scopus 로고
    • Analysis of mechanism and kinetics of thermal inactivation of enzymes: Evaluation of multitemperature data applied to inactivation of yeast invertase
    • Vrábel P., Polakovič M., Štefuca V., Báleš V. Analysis of mechanism and kinetics of thermal inactivation of enzymes: evaluation of multitemperature data applied to inactivation of yeast invertase. Enzyme Microb. Technol. 20:1997b;348-354.
    • (1997) Enzyme Microb. Technol. , vol.20 , pp. 348-354
    • Vrábel, P.1    Polakovič, M.2    Štefuca, V.3    Báleš, V.4
  • 19
    • 0023792713 scopus 로고
    • Trace level analysis for mercury using urease in combination with an ammonia gas sensitive semiconductor structure
    • Winquist F., Lundstroem L., Danielsson B. Trace level analysis for mercury using urease in combination with an ammonia gas sensitive semiconductor structure. Anal. Lett. B. 21:1988;1801-1816.
    • (1988) Anal. Lett. B , vol.21 , pp. 1801-1816
    • Winquist, F.1    Lundstroem, L.2    Danielsson, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.