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Volumn 38, Issue 3, 2006, Pages 347-353

Evaluation of radish (Raphanus sativus L.) peroxidase activity after high-pressure treatment with carbon dioxide

Author keywords

Compressed CO2; Peroxidase; Radish; Specific activity; Water content

Indexed keywords

DEPRESSURIZATION; PEROXIDASE; SPECIFIC ACTIVITY; WATER CONTENT;

EID: 33749650548     PISSN: 08968446     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.supflu.2005.11.019     Document Type: Article
Times cited : (46)

References (45)
  • 1
    • 0003514551 scopus 로고    scopus 로고
    • John Wiley and Sons, New York 18-25
    • Dunford H.B. Heme Peroxidases (1999), John Wiley and Sons, New York 18-25
    • (1999) Heme Peroxidases
    • Dunford, H.B.1
  • 2
    • 5644272649 scopus 로고    scopus 로고
    • Oxidation of carboxylic acids by horseradish peroxidase in prosthetic heme modification and inactivation
    • Huang L., Colas C., and Ortiz de Montellano P.R. Oxidation of carboxylic acids by horseradish peroxidase in prosthetic heme modification and inactivation. J. Am. Chem. Soc. 126 (2004) 12865-12873
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 12865-12873
    • Huang, L.1    Colas, C.2    Ortiz de Montellano, P.R.3
  • 3
    • 17644409007 scopus 로고    scopus 로고
    • Prosthetic heme modification during halide ion oxidation. Demonstration of chloride oxidation by horseradish peroxidase
    • Huang L., Wojciechowski G., and Ortiz de Montellano P.R. Prosthetic heme modification during halide ion oxidation. Demonstration of chloride oxidation by horseradish peroxidase. J. Am. Chem. Soc. 127 (2005) 5345-5353
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 5345-5353
    • Huang, L.1    Wojciechowski, G.2    Ortiz de Montellano, P.R.3
  • 5
    • 0037070477 scopus 로고    scopus 로고
    • Effective oxygen transfer reaction catalyzed by microperoxidase-11 during sulfur oxidation of dibenzothiophene
    • Ichinose H., Wariishi H., and Tanaka H. Effective oxygen transfer reaction catalyzed by microperoxidase-11 during sulfur oxidation of dibenzothiophene. Enzyme Microb. Technol. 30 (2002) 334-339
    • (2002) Enzyme Microb. Technol. , vol.30 , pp. 334-339
    • Ichinose, H.1    Wariishi, H.2    Tanaka, H.3
  • 6
    • 1942439106 scopus 로고    scopus 로고
    • Biocatalitic oxidation of primary and secondary alcohols
    • Kroutil W., Mang H., Edegger K., and Faber K. Biocatalitic oxidation of primary and secondary alcohols. Adv. Synth. Catal. 346 (2004) 125-142
    • (2004) Adv. Synth. Catal. , vol.346 , pp. 125-142
    • Kroutil, W.1    Mang, H.2    Edegger, K.3    Faber, K.4
  • 7
    • 1842583994 scopus 로고    scopus 로고
    • Recent advances in the biocatalitic reduction of ketones and oxidation of sec-alcohols
    • Kroutil W., Mang H., Edegger K., and Faber K. Recent advances in the biocatalitic reduction of ketones and oxidation of sec-alcohols. Curr. Opin. Chem. Biol. 8 (2004) 120-126
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 120-126
    • Kroutil, W.1    Mang, H.2    Edegger, K.3    Faber, K.4
  • 9
    • 0342803204 scopus 로고    scopus 로고
    • Purification and partial characterization of three turnip (Brassica napus L. Var. Esculenta D. C.) peroxidades
    • Duarte-Vázquez M.A., Garcia-Almendárez B., Regalado C., and Whitaker J.R. Purification and partial characterization of three turnip (Brassica napus L. Var. Esculenta D. C.) peroxidades. J. Agric. Food. Chem. 48 (2000) 1574-1579
    • (2000) J. Agric. Food. Chem. , vol.48 , pp. 1574-1579
    • Duarte-Vázquez, M.A.1    Garcia-Almendárez, B.2    Regalado, C.3    Whitaker, J.R.4
  • 11
    • 84949060197 scopus 로고
    • Enzymes in organic synthesis-alteration of reversible reactions to irreversible processes
    • Fang J.M., and Wong C.H. Enzymes in organic synthesis-alteration of reversible reactions to irreversible processes. Synlett 6 (1994) 393-402
    • (1994) Synlett , vol.6 , pp. 393-402
    • Fang, J.M.1    Wong, C.H.2
  • 12
    • 0026139064 scopus 로고
    • Enzymatic catalysis on coal-related compounds in organic media: kinetics and potencial commercial applications
    • Dordick J.S., Ryu K., and McEldoon J. Enzymatic catalysis on coal-related compounds in organic media: kinetics and potencial commercial applications. Resour. Conserv. Recy. 5 (1991) 195-209
    • (1991) Resour. Conserv. Recy. , vol.5 , pp. 195-209
    • Dordick, J.S.1    Ryu, K.2    McEldoon, J.3
  • 13
    • 0028928260 scopus 로고
    • Enzyme memory-what is remembered and why
    • Klibanov A.M. Enzyme memory-what is remembered and why. Nature 374 (1995) 596-599
    • (1995) Nature , vol.374 , pp. 596-599
    • Klibanov, A.M.1
  • 14
    • 0346854239 scopus 로고    scopus 로고
    • Enzyme-catalyzed reactions in dense gases
    • Knez Z., Habulin M., and Krmelj V. Enzyme-catalyzed reactions in dense gases. J. Supercrit. Fluid 14 (1998) 17-29
    • (1998) J. Supercrit. Fluid , vol.14 , pp. 17-29
    • Knez, Z.1    Habulin, M.2    Krmelj, V.3
  • 15
    • 0036099668 scopus 로고    scopus 로고
    • Compressed gases as alternative enzymatic-reaction solvents: a short review
    • Knez Z., and Habulin M. Compressed gases as alternative enzymatic-reaction solvents: a short review. J. Supercrit. Fluid 23 (2002) 29-42
    • (2002) J. Supercrit. Fluid , vol.23 , pp. 29-42
    • Knez, Z.1    Habulin, M.2
  • 18
    • 0037467466 scopus 로고    scopus 로고
    • Water activity effects on geranyl acetate synthesis catalyzed by novozym in supercritical ethane and in supercritical carbon dioxide
    • Peres C., Da Silva M.D.R.G., and Barreiros S. Water activity effects on geranyl acetate synthesis catalyzed by novozym in supercritical ethane and in supercritical carbon dioxide. J. Agric. Food Chem. 51 (2003) 1884-1888
    • (2003) J. Agric. Food Chem. , vol.51 , pp. 1884-1888
    • Peres, C.1    Da Silva, M.D.R.G.2    Barreiros, S.3
  • 19
    • 0029111630 scopus 로고
    • Biocatalytic synthesis of acrylates in organic solvents and supercritical fluids. III. Does carbon dioxide covalently modify enzymes
    • Kamat S., Critchley G., Beckman E.J., and Russel A.J. Biocatalytic synthesis of acrylates in organic solvents and supercritical fluids. III. Does carbon dioxide covalently modify enzymes. Biotechnol. Bioeng. 46 (1995) 610-620
    • (1995) Biotechnol. Bioeng. , vol.46 , pp. 610-620
    • Kamat, S.1    Critchley, G.2    Beckman, E.J.3    Russel, A.J.4
  • 21
    • 0344507541 scopus 로고    scopus 로고
    • Metalloporphyrin-catalysed homogeneous oxidation in supercritical carbon dioxide
    • Birnbaum E.R., LeLacher R.M., Horton A.C., and Tumas W. Metalloporphyrin-catalysed homogeneous oxidation in supercritical carbon dioxide. J. Mol. Catal. 139 (1999) 11-24
    • (1999) J. Mol. Catal. , vol.139 , pp. 11-24
    • Birnbaum, E.R.1    LeLacher, R.M.2    Horton, A.C.3    Tumas, W.4
  • 23
    • 0029869349 scopus 로고    scopus 로고
    • Effect of high-pressure treatment on the activity of some polyphenoloxidases
    • Gomes M.R.A., and Ledward D.A. Effect of high-pressure treatment on the activity of some polyphenoloxidases. Food Chem. 56 (1996) 1-5
    • (1996) Food Chem. , vol.56 , pp. 1-5
    • Gomes, M.R.A.1    Ledward, D.A.2
  • 24
    • 0030864450 scopus 로고    scopus 로고
    • Effects of high pressure processing on polyphenoloxidase enzyme activity of grape musts
    • Castellari M., Matricardi L., Arfelli G., Rovere P., and Amati A. Effects of high pressure processing on polyphenoloxidase enzyme activity of grape musts. Food Chem. 60 (1997) 647-649
    • (1997) Food Chem. , vol.60 , pp. 647-649
    • Castellari, M.1    Matricardi, L.2    Arfelli, G.3    Rovere, P.4    Amati, A.5
  • 25
    • 3042648626 scopus 로고    scopus 로고
    • The effects of high hydrostatic pressure on β-glucosidase, peroxidase and polyphenoloxidase in red rapberry (Rubus idaeus) and strawberry (Fragaria × ananassa)
    • Garcia-Palazon A., Suthanthangjai W., Kajda P., and Zabetakis I. The effects of high hydrostatic pressure on β-glucosidase, peroxidase and polyphenoloxidase in red rapberry (Rubus idaeus) and strawberry (Fragaria × ananassa). Food Chem. 88 (2004) 7-10
    • (2004) Food Chem. , vol.88 , pp. 7-10
    • Garcia-Palazon, A.1    Suthanthangjai, W.2    Kajda, P.3    Zabetakis, I.4
  • 26
    • 0036751941 scopus 로고    scopus 로고
    • Mechanism-based irreversible inactivation of horseradish peroxidase at 500 MPa
    • García A.F., Butz P., and Tauscher B. Mechanism-based irreversible inactivation of horseradish peroxidase at 500 MPa. Biotechnol. Prog. 18 (2002) 1076-1081
    • (2002) Biotechnol. Prog. , vol.18 , pp. 1076-1081
    • García, A.F.1    Butz, P.2    Tauscher, B.3
  • 27
    • 0035198407 scopus 로고    scopus 로고
    • Activity and stability of lipases from different sources in supercritical carbon dioxide and near-critical propane
    • Habulin M., and Knez Z. Activity and stability of lipases from different sources in supercritical carbon dioxide and near-critical propane. J. Chem. Technol. Biotechnol. 76 (2001) 1260-1266
    • (2001) J. Chem. Technol. Biotechnol. , vol.76 , pp. 1260-1266
    • Habulin, M.1    Knez, Z.2
  • 28
    • 0036568363 scopus 로고    scopus 로고
    • Inactivation of lipase by carbon dioxide under atmospheric pressure
    • Fadíloǧlu S., and Erkmen O. Inactivation of lipase by carbon dioxide under atmospheric pressure. J. Food Eng. 52 (2002) 331-335
    • (2002) J. Food Eng. , vol.52 , pp. 331-335
    • Fadíloǧlu, S.1    Erkmen, O.2
  • 31
    • 0006625588 scopus 로고    scopus 로고
    • A simple process for increasing the specific activity of porcine pancreatic lipase by supercritical carbon dioxide treatment
    • Gießauf A., and Gamse T. A simple process for increasing the specific activity of porcine pancreatic lipase by supercritical carbon dioxide treatment. J. Mol. Catal. B: Enzymat. 9 (2000) 57-64
    • (2000) J. Mol. Catal. B: Enzymat. , vol.9 , pp. 57-64
    • Gießauf, A.1    Gamse, T.2
  • 32
    • 0002185333 scopus 로고
    • Effect of treatment with supercritical carbon dioxide on enzymatic activity
    • Taniguchi M., Kamihira M., and Kobayashi T. Effect of treatment with supercritical carbon dioxide on enzymatic activity. Agric. Biol. Chem. 51 (1987) 593-594
    • (1987) Agric. Biol. Chem. , vol.51 , pp. 593-594
    • Taniguchi, M.1    Kamihira, M.2    Kobayashi, T.3
  • 33
    • 38249030929 scopus 로고
    • Effective utilisation of horseradish and wasabi by treatment with supercritical carbon dioxide
    • Taniguchi M., Nomura R., Kamihira M., Kijima I., and Kobayashi T. Effective utilisation of horseradish and wasabi by treatment with supercritical carbon dioxide. J. Ferment. Technol. 66 (1988) 347-353
    • (1988) J. Ferment. Technol. , vol.66 , pp. 347-353
    • Taniguchi, M.1    Nomura, R.2    Kamihira, M.3    Kijima, I.4    Kobayashi, T.5
  • 34
    • 17144435609 scopus 로고    scopus 로고
    • Uso analítico de tecidos e de extratos brutos vegetais como fonte enzimática
    • Fatibello-Filho O., and Vieira I.C. Uso analítico de tecidos e de extratos brutos vegetais como fonte enzimática. Quím. Nova 25 (2002) 455-464
    • (2002) Quím. Nova , vol.25 , pp. 455-464
    • Fatibello-Filho, O.1    Vieira, I.C.2
  • 35
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 36
    • 0031571165 scopus 로고    scopus 로고
    • Identification of the colored guaiacol oxidation product produced by peroxidases
    • Doerge D.R., Divi R.L., and Churchwell M.I. Identification of the colored guaiacol oxidation product produced by peroxidases. Anal. Biochem. 250 (1997) 10-17
    • (1997) Anal. Biochem. , vol.250 , pp. 10-17
    • Doerge, D.R.1    Divi, R.L.2    Churchwell, M.I.3
  • 38
    • 0003595944 scopus 로고
    • Angus S., Armstrong B., and Reuck K.M. (Eds), Pergamon Press, Oxford, UK (Chapter 2)
    • In: Angus S., Armstrong B., and Reuck K.M. (Eds). International Thermodynamic Tables of the Fluid State: Carbon Dioxide (1976), Pergamon Press, Oxford, UK 340 (Chapter 2)
    • (1976) International Thermodynamic Tables of the Fluid State: Carbon Dioxide , pp. 340
  • 39
    • 0024694327 scopus 로고
    • Activation thermodynamics of the binding of carbon monoxide to horseradish peroxidase. Role of pressure, temperature and solvent
    • Balny C., and Travers F. Activation thermodynamics of the binding of carbon monoxide to horseradish peroxidase. Role of pressure, temperature and solvent. Biophys. Chem. 33 (1989) 237-244
    • (1989) Biophys. Chem. , vol.33 , pp. 237-244
    • Balny, C.1    Travers, F.2
  • 41
    • 0021679466 scopus 로고
    • A hypotesis on the role of pressure in the origin of life
    • Nickerson K.W. A hypotesis on the role of pressure in the origin of life. J. Theor. Biol. 110 (1984) 487-499
    • (1984) J. Theor. Biol. , vol.110 , pp. 487-499
    • Nickerson, K.W.1
  • 42
    • 10144249599 scopus 로고    scopus 로고
    • Application of high hydrostatic pressure for increasing activity and stability of enzymes
    • Mozhaev V.V., Lange R., Kudryashova E.V., and Balny C. Application of high hydrostatic pressure for increasing activity and stability of enzymes. Biotechnol. Bioeng. 52 (1996) 320-331
    • (1996) Biotechnol. Bioeng. , vol.52 , pp. 320-331
    • Mozhaev, V.V.1    Lange, R.2    Kudryashova, E.V.3    Balny, C.4
  • 43
    • 0342325481 scopus 로고
    • Pressure inactivation of alpha-chymotrypsin
    • Taniguchi Y., and Suzuki K. Pressure inactivation of alpha-chymotrypsin. J. Phys. Chem. 87 (1983) 5185-5193
    • (1983) J. Phys. Chem. , vol.87 , pp. 5185-5193
    • Taniguchi, Y.1    Suzuki, K.2
  • 44
    • 0342813156 scopus 로고    scopus 로고
    • Structural properties of peroxidases
    • Banci L. Structural properties of peroxidases. J. Biotechnol. 53 (1997) 253-263
    • (1997) J. Biotechnol. , vol.53 , pp. 253-263
    • Banci, L.1
  • 45
    • 0000364710 scopus 로고
    • 2: stabilizing effect of S{single bond}S bonds during the depressurization step
    • 2: stabilizing effect of S{single bond}S bonds during the depressurization step. Biotechnol. Lett. 10 (1988) 569-574
    • (1988) Biotechnol. Lett. , vol.10 , pp. 569-574
    • Kasche, V.1    Schlothauer, R.2    Brunner, G.3


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