메뉴 건너뛰기




Volumn 55, Issue 24, 2007, Pages 9739-9749

A review on spectrophotometric methods for measuring the monophenolase and diphenolase activities of tyrosinase

Author keywords

Diphenolase; Monophenolase; Polyphenol oxidase; Spectrophotometric methods; Tyrosinase

Indexed keywords

CATECHOL OXIDASE; MONOPHENOL MONOOXYGENASE; OXIDOREDUCTASE;

EID: 37349053743     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf0712301     Document Type: Review
Times cited : (128)

References (61)
  • 1
    • 0003557568 scopus 로고    scopus 로고
    • Nordlund, J. J, Boissy, R, Hearing, V, King, R, Ortonne, J. P, Eds, University Press: Oxford
    • Prota, M. G.; d'Ischia, A.; Napolitano, A. In The Pigmentary System; Nordlund, J. J.; Boissy, R., Hearing, V., King, R., Ortonne, J. P., Eds.; University Press: Oxford, 1988.
    • (1988) The Pigmentary System
    • Prota, M.G.1    d'Ischia, A.2    Napolitano, A.3
  • 2
    • 7744236144 scopus 로고    scopus 로고
    • Solomon, E. I.; Sundaram, U. M.; Machonkin, T. E. Multicopper oxidases and oxygenases. Chem. Rev. 1996, 96, 2563-2606.
    • Solomon, E. I.; Sundaram, U. M.; Machonkin, T. E. Multicopper oxidases and oxygenases. Chem. Rev. 1996, 96, 2563-2606.
  • 3
    • 4544340747 scopus 로고    scopus 로고
    • Functional changes in the family of type 3 copper proteins during evolution
    • Jaenicke, E.; Decker, H. Functional changes in the family of type 3 copper proteins during evolution. ChemBioChem 2004, 5, 163-169.
    • (2004) ChemBioChem , vol.5 , pp. 163-169
    • Jaenicke, E.1    Decker, H.2
  • 4
    • 0035905357 scopus 로고    scopus 로고
    • Oxygen binding, activation, and reduction to water by copper proteins
    • Solomon, E. I.; Chen, P.; Metz, M.; Lee, S. K.; Palmer, A. E. Oxygen binding, activation, and reduction to water by copper proteins. Angew. Chem., Int. Ed. 2001, 40, 4570-4590.
    • (2001) Angew. Chem., Int. Ed , vol.40 , pp. 4570-4590
    • Solomon, E.I.1    Chen, P.2    Metz, M.3    Lee, S.K.4    Palmer, A.E.5
  • 5
    • 0027981519 scopus 로고
    • Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences
    • Magnus, K. A.; Hazes, B.; Ton-That, H.; Bonaventura, C.; Bonaventura, J.; Hol, W. G. Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences. Proteins 1994, 19, 302-309.
    • (1994) Proteins , vol.19 , pp. 302-309
    • Magnus, K.A.1    Hazes, B.2    Ton-That, H.3    Bonaventura, C.4    Bonaventura, J.5    Hol, W.G.6
  • 6
    • 0032525161 scopus 로고    scopus 로고
    • Crystal structure of a functional unit from Octopus hemocyanin
    • Cuff, M. E.; Miller, K. I.; van Holde, K. E.; Hendrickson, W. A. Crystal structure of a functional unit from Octopus hemocyanin. J. Mol. Biol. 1998, 278, 855-870.
    • (1998) J. Mol. Biol , vol.278 , pp. 855-870
    • Cuff, M.E.1    Miller, K.I.2    van Holde, K.E.3    Hendrickson, W.A.4
  • 7
    • 0031760504 scopus 로고    scopus 로고
    • Cristal structure of a plant catechol oxidase containing a dicopper center
    • Klabunde, T.; Eicken, C.; Sacchettini, J. C.; Krebs, B. Cristal structure of a plant catechol oxidase containing a dicopper center. Nat. Struct. Biol. 1998, 5, 1084-1090.
    • (1998) Nat. Struct. Biol , vol.5 , pp. 1084-1090
    • Klabunde, T.1    Eicken, C.2    Sacchettini, J.C.3    Krebs, B.4
  • 9
    • 33646827679 scopus 로고    scopus 로고
    • Crystallographic evidence that the dinuclear cooper center of tyrosinase is flexible during catalysis
    • Matoba, Y.; Kumagai, T.; Yamamoto, A.; Yoshitsu, H.; Sugiyama, M. Crystallographic evidence that the dinuclear cooper center of tyrosinase is flexible during catalysis. J. Biol. Chem. 2006, 281, 8981-8990.
    • (2006) J. Biol. Chem , vol.281 , pp. 8981-8990
    • Matoba, Y.1    Kumagai, T.2    Yamamoto, A.3    Yoshitsu, H.4    Sugiyama, M.5
  • 10
    • 0042415543 scopus 로고    scopus 로고
    • Physiochemical properties and function of plant polyphenol oxidase: A review
    • Yoruk, R.; Marshall, M. R. Physiochemical properties and function of plant polyphenol oxidase: a review. J. Food Chem. 2003, 27, 361-422.
    • (2003) J. Food Chem , vol.27 , pp. 361-422
    • Yoruk, R.1    Marshall, M.R.2
  • 12
    • 33749517866 scopus 로고    scopus 로고
    • Polyphenol oxidases in plants and fungi: Going places? A review
    • Mayer, A. M. Polyphenol oxidases in plants and fungi: Going places? A review. Phytochemistry 2006, 67, 2318-2331.
    • (2006) Phytochemistry , vol.67 , pp. 2318-2331
    • Mayer, A.M.1
  • 13
    • 33645163110 scopus 로고    scopus 로고
    • Fungal tyrosinases: New prospects in molecular characteristics bioengineering and biotechnological applications
    • Halaouli, S.; Asther, M.; Sigoillot, J. C.; Hamdi, M.; Lomascolo, A. Fungal tyrosinases: new prospects in molecular characteristics bioengineering and biotechnological applications. J. Appl. Microbiol. 2006, 100, 219-232.
    • (2006) J. Appl. Microbiol , vol.100 , pp. 219-232
    • Halaouli, S.1    Asther, M.2    Sigoillot, J.C.3    Hamdi, M.4    Lomascolo, A.5
  • 15
    • 0014010123 scopus 로고
    • The tyrosine hydroxylase activity of mammalian tyrosinase
    • Pomerantz, S. H. The tyrosine hydroxylase activity of mammalian tyrosinase. J. Biol. Chem. 1966, 241, 161-168.
    • (1966) J. Biol. Chem , vol.241 , pp. 161-168
    • Pomerantz, S.H.1
  • 16
    • 0017112928 scopus 로고
    • A sensitive new assay for the oxidation of 3,4-dihydroxy-L-phenylalanine by tyrosinase
    • Pomerantz, S. H. A sensitive new assay for the oxidation of 3,4-dihydroxy-L-phenylalanine by tyrosinase. Anal. Biochem. 1976, 75, 86-90.
    • (1976) Anal. Biochem , vol.75 , pp. 86-90
    • Pomerantz, S.H.1
  • 17
    • 0026645649 scopus 로고
    • Calibration of a clark-type oxygen electrode by tyrosinase-catalyzed oxidation of 4-tert-butylcatechol
    • Rodriguez-López, J. N.; Ros Martinez, J. R.; Varón, R.; García-Cánovas, F. Calibration of a clark-type oxygen electrode by tyrosinase-catalyzed oxidation of 4-tert-butylcatechol. Anal. Biochem. 1992, 202, 356-360.
    • (1992) Anal. Biochem , vol.202 , pp. 356-360
    • Rodriguez-López, J.N.1    Ros Martinez, J.R.2    Varón, R.3    García-Cánovas, F.4
  • 18
    • 0022416873 scopus 로고
    • An electrometric method for the determination of tyrosinase activity
    • Solano-Muñoz, F.; Peñafiel, R.; Galindo, J. D. An electrometric method for the determination of tyrosinase activity. Biochem. J. 1985, 229, 573-578.
    • (1985) Biochem. J , vol.229 , pp. 573-578
    • Solano-Muñoz, F.1    Peñafiel, R.2    Galindo, J.D.3
  • 19
    • 33947438134 scopus 로고
    • A new method for the measurement of tyrosinase catecholase activity
    • Miller, H. W.; Dawson, C. R. A new method for the measurement of tyrosinase catecholase activity. J. Am. Chem. Soc. 1941, 63, 3375-3382.
    • (1941) J. Am. Chem. Soc , vol.63 , pp. 3375-3382
    • Miller, H.W.1    Dawson, C.R.2
  • 20
    • 0012159487 scopus 로고
    • A new method for the measurement of tyrosinase catecholase activity II, catecholase activity based on the initial reaction velocity
    • Miller, H. W.; Mallette, M. F.; Roth, L. J.; Dawson, C. R. A new method for the measurement of tyrosinase catecholase activity II, catecholase activity based on the initial reaction velocity. J. Am. Chem. Soc. 1944, 66, 514-519.
    • (1944) J. Am. Chem. Soc , vol.66 , pp. 514-519
    • Miller, H.W.1    Mallette, M.F.2    Roth, L.J.3    Dawson, C.R.4
  • 21
    • 0001178114 scopus 로고
    • A spectrophotometric method for the determination of the catecholase activity of tyrosinase and some of its applications
    • El-Bayoumi, M. A.; Frieden, E. A spectrophotometric method for the determination of the catecholase activity of tyrosinase and some of its applications. J. Am. Chem. Soc. 1957, 79, 4854-4858.
    • (1957) J. Am. Chem. Soc , vol.79 , pp. 4854-4858
    • El-Bayoumi, M.A.1    Frieden, E.2
  • 22
    • 0015611566 scopus 로고
    • A spectrophotometric method for the determination of the cathecholase activity of tyrosinase by Besthorn's hydrazone
    • Pifferi, P. G.; Baldassari, L. A spectrophotometric method for the determination of the cathecholase activity of tyrosinase by Besthorn's hydrazone. Anal. Biochem. 1973, 52, 325-335.
    • (1973) Anal. Biochem , vol.52 , pp. 325-335
    • Pifferi, P.G.1    Baldassari, L.2
  • 23
    • 0016040099 scopus 로고
    • Inhibition by carboxylic acids of an o-diphenol oxidase from Prunus avium fruits
    • Pifferi, P. G.; Baldassari, L.; Cultrera, R. Inhibition by carboxylic acids of an o-diphenol oxidase from Prunus avium fruits. J. Sci. Food Agric. 1974, 25, 263-270.
    • (1974) J. Sci. Food Agric , vol.25 , pp. 263-270
    • Pifferi, P.G.1    Baldassari, L.2    Cultrera, R.3
  • 24
    • 0017165709 scopus 로고
    • An improvement of the spectrophotometric method for the determination of tyrosinase catecholase activity by Besthorn's hydrazone
    • Mazzocco, F.; Pifferi, P. G. An improvement of the spectrophotometric method for the determination of tyrosinase catecholase activity by Besthorn's hydrazone. Anal. Biochem. 1976, 72, 643-647.
    • (1976) Anal. Biochem , vol.72 , pp. 643-647
    • Mazzocco, F.1    Pifferi, P.G.2
  • 25
    • 0018388959 scopus 로고
    • A new spectrophotometric method for the determination of cresolase activity of epidermis tyrosinase
    • García-Carmona, F.; Pedreño, E.; Galindo, J. D.; García-Cánovas, F. A new spectrophotometric method for the determination of cresolase activity of epidermis tyrosinase. Anal. Biochem. 1979, 95, 433-435.
    • (1979) Anal. Biochem , vol.95 , pp. 433-435
    • García-Carmona, F.1    Pedreño, E.2    Galindo, J.D.3    García-Cánovas, F.4
  • 30
    • 0022057370 scopus 로고
    • A spectrophotometric assay for mammalian tyrosinase utilizing the formation of melanochrome from L-dopa
    • Vachtenheim, J.; Duchon, J.; Matous, B. A spectrophotometric assay for mammalian tyrosinase utilizing the formation of melanochrome from L-dopa. Anal. Biochem. 1985, 146, 405-410.
    • (1985) Anal. Biochem , vol.146 , pp. 405-410
    • Vachtenheim, J.1    Duchon, J.2    Matous, B.3
  • 31
    • 0023374402 scopus 로고
    • Kinetic study of the transient phase of a chemical reaction system coupled to an enzymatically catalized step: Application to the oxidation of epinine by tyrosinase
    • Escribano, J.; García, M.; García-Cánovas, F.; García-Carmona, F.; Varón, R.; Tudela, J.; Lozano, J. A. Kinetic study of the transient phase of a chemical reaction system coupled to an enzymatically catalized step: Application to the oxidation of epinine by tyrosinase. Biophys. Chem. 1987, 27, 15-25.
    • (1987) Biophys. Chem , vol.27 , pp. 15-25
    • Escribano, J.1    García, M.2    García-Cánovas, F.3    García-Carmona, F.4    Varón, R.5    Tudela, J.6    Lozano, J.A.7
  • 32
    • 0024342694 scopus 로고
    • A chromogenic assay for catecholoxidases based on the addition of L-proline to o-quinones
    • Rzepecki, L. M.; Waite, J. H. A chromogenic assay for catecholoxidases based on the addition of L-proline to o-quinones. Anal. Biochem. 1989, 179, 375-381.
    • (1989) Anal. Biochem , vol.179 , pp. 375-381
    • Rzepecki, L.M.1    Waite, J.H.2
  • 33
    • 0025910929 scopus 로고
    • New assays for the tyrosine hydroxylase and dopa oxidase activities of tyrosinase
    • Winder, A. J.; Harris, H. New assays for the tyrosine hydroxylase and dopa oxidase activities of tyrosinase. Eur. J. Biochem. 1991, 198, 317-326.
    • (1991) Eur. J. Biochem , vol.198 , pp. 317-326
    • Winder, A.J.1    Harris, H.2
  • 34
    • 0025875042 scopus 로고
    • A continuous spectrophotometric method for the determination of diphenolase activity of tyrosinase using 3,4-dihydroxymandelic acid
    • Rodríguez-Lopez, J. N.; Serna Rodríguez, P.; Tudela, J.; Varon, R.; García-Cánovas, F. A continuous spectrophotometric method for the determination of diphenolase activity of tyrosinase using 3,4-dihydroxymandelic acid. Anal. Biochem. 1991, 195, 369-374.
    • (1991) Anal. Biochem , vol.195 , pp. 369-374
    • Rodríguez-Lopez, J.N.1    Serna Rodríguez, P.2    Tudela, J.3    Varon, R.4    García-Cánovas, F.5
  • 35
  • 36
    • 0028180674 scopus 로고
    • A stopped spectrophotometric assay for the dopa oxidase activity of tyrosinase
    • Winder, A. J. A stopped spectrophotometric assay for the dopa oxidase activity of tyrosinase. J. Biochem. Biophys. Methods 1994, 28, 173-183.
    • (1994) J. Biochem. Biophys. Methods , vol.28 , pp. 173-183
    • Winder, A.J.1
  • 39
    • 0027440538 scopus 로고
    • New spectrophotometric assay for polyphenol oxidase activity
    • Gauillard, F.; Richard-Forget, F.; Nicolas, J. New spectrophotometric assay for polyphenol oxidase activity. Anal. Biochem. 1993, 215, 59-65.
    • (1993) Anal. Biochem , vol.215 , pp. 59-65
    • Gauillard, F.1    Richard-Forget, F.2    Nicolas, J.3
  • 41
    • 0009160591 scopus 로고
    • A comparison of mushroom tyrosinase dopaquinone and dopachrome assays using diode-array spectrophotometric; dopachrome formation vs a ascorbate-linked dopaquinone reduction
    • Behbahani, I.; Miller, S. A.; O'Keeffe, D. H. A comparison of mushroom tyrosinase dopaquinone and dopachrome assays using diode-array spectrophotometric; dopachrome formation vs a ascorbate-linked dopaquinone reduction. Microchem. J. 1993, 47, 251-260.
    • (1993) Microchem. J , vol.47 , pp. 251-260
    • Behbahani, I.1    Miller, S.A.2    O'Keeffe, D.H.3
  • 42
    • 0344739850 scopus 로고    scopus 로고
    • A new continuous spectrophotometric assay method for dopa oxidase activity of tyrosinase
    • Park, Y. D.; Lee, J. R.; Park, K. H.; Hah, H. S.; Hahn, M. J.; Yang, J. M. A new continuous spectrophotometric assay method for dopa oxidase activity of tyrosinase. J. Protein Chem. 2003, 22, 473-180.
    • (2003) J. Protein Chem , vol.22 , pp. 473-180
    • Park, Y.D.1    Lee, J.R.2    Park, K.H.3    Hah, H.S.4    Hahn, M.J.5    Yang, J.M.6
  • 43
    • 0037216767 scopus 로고    scopus 로고
    • Direct spectrophotometric assay of monooxygenase and oxidase activities of mushroom tyrosinase in the presence of synthetic and natural substrates
    • Haghbeen, K.; Tan, E. W. Direct spectrophotometric assay of monooxygenase and oxidase activities of mushroom tyrosinase in the presence of synthetic and natural substrates. Anal. Biochem. 2003, 312, 23-32.
    • (2003) Anal. Biochem , vol.312 , pp. 23-32
    • Haghbeen, K.1    Tan, E.W.2
  • 45
    • 0003557568 scopus 로고    scopus 로고
    • Advances in Enzymatic Analysis of Melanogenesis
    • Nordlund, J. J, Ed, Oxford University Press: New York
    • Solano, F.; García-Borrón, J. C. Advances in Enzymatic Analysis of Melanogenesis. In The Pigmentary System, physiology and Patophysiology; Nordlund, J. J., Ed.; Oxford University Press: New York, 1998; pp 467-471.
    • (1998) The Pigmentary System, physiology and Patophysiology , pp. 467-471
    • Solano, F.1    García-Borrón, J.C.2
  • 47
    • 0014939358 scopus 로고
    • Physicochemical and kinetic properties of mushroom tyrosinase
    • Duckworth, H. W.; Coleman, J. E. Physicochemical and kinetic properties of mushroom tyrosinase. J. Biol. Chem. 1970, 245, 1613-1625.
    • (1970) J. Biol. Chem , vol.245 , pp. 1613-1625
    • Duckworth, H.W.1    Coleman, J.E.2
  • 51
    • 0027453615 scopus 로고
    • Effect of L-ascorbic acid on the monophenolase activity of tyrosinase
    • Ros, J. R.; Rodriguez-Lopez, J. N.; García-Cánovas, F. Effect of L-ascorbic acid on the monophenolase activity of tyrosinase. Biochem. J. 1993, 295, 309-12.
    • (1993) Biochem. J , vol.295 , pp. 309-312
    • Ros, J.R.1    Rodriguez-Lopez, J.N.2    García-Cánovas, F.3
  • 53
    • 0036887577 scopus 로고    scopus 로고
    • Kinetic characterization of the reaction mechanism of mushroom tyrosinase on tyramine/dopamine and L-tyrosine methyl esther/L-dopa methyl esther
    • Fenoll, L. G.; Rodriguez-Lopez, J. N.; Varón, R.; García-Ruíz, P. A.; García-Cánovas, F.; Tudela, J. Kinetic characterization of the reaction mechanism of mushroom tyrosinase on tyramine/dopamine and L-tyrosine methyl esther/L-dopa methyl esther. Int. J. Biochem. Cell Biol. 2002, 34, 1594-1607.
    • (2002) Int. J. Biochem. Cell Biol , vol.34 , pp. 1594-1607
    • Fenoll, L.G.1    Rodriguez-Lopez, J.N.2    Varón, R.3    García-Ruíz, P.A.4    García-Cánovas, F.5    Tudela, J.6
  • 55
    • 0027973584 scopus 로고
    • A substrate recycling assay for phenolic compounds using tyrosinase and NADH
    • Brown, R. S.; Male, K. B.; Luong, J. H. A substrate recycling assay for phenolic compounds using tyrosinase and NADH. Anal. Biochem. 1994, 222, 131-139.
    • (1994) Anal. Biochem , vol.222 , pp. 131-139
    • Brown, R.S.1    Male, K.B.2    Luong, J.H.3
  • 57
    • 0032524470 scopus 로고    scopus 로고
    • 4-Hydroxianisole: The most suitable monophenolic substrate for determining spectrophotometrically the monophenolase activity of polyphenol oxidase from fruits and vegetables
    • Espín, J. C.; Tudela, J.; García-Cánovas, F. 4-Hydroxianisole: The most suitable monophenolic substrate for determining spectrophotometrically the monophenolase activity of polyphenol oxidase from fruits and vegetables. Anal. Biochem. 1998, 259, 118-126.
    • (1998) Anal. Biochem , vol.259 , pp. 118-126
    • Espín, J.C.1    Tudela, J.2    García-Cánovas, F.3
  • 58
  • 60
    • 0033983446 scopus 로고    scopus 로고
    • Use of a windows program for simulation of the progress curves of reactants and intermediates involved in enzyme-catalyzed reactions
    • García-Sevilla, F.; Garrido del Solo, C.; Duggleby, R. G.; García-Cánovas, F.; Peyro, R.; Varón, R. Use of a windows program for simulation of the progress curves of reactants and intermediates involved in enzyme-catalyzed reactions. Biosystems 2000, 54, 151-164.
    • (2000) Biosystems , vol.54 , pp. 151-164
    • García-Sevilla, F.1    Garrido del Solo, C.2    Duggleby, R.G.3    García-Cánovas, F.4    Peyro, R.5    Varón, R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.