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Volumn 61, Issue 6, 1996, Pages 1177-1182

Continuous spectrophotometric method for determining monophenolase and diphenolase activities of pear polyphenoloxidase

Author keywords

Diphenols; MBTH; Monophenols; Pear; Polyphenoloxidase

Indexed keywords


EID: 0030444246     PISSN: 00221147     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2621.1996.tb10955.x     Document Type: Article
Times cited : (56)

References (45)
  • 1
    • 0019300258 scopus 로고
    • Guidelines for data acquisition and data quality evaluation in environmental chemistry
    • ACS Committee on Environmental Improvement and Subcommittee on Environmental Analytical Chemistry. 1980. Guidelines for data acquisition and data quality evaluation in environmental chemistry. Anal. Chem. 52: 2242-2249.
    • (1980) Anal. Chem. , vol.52 , pp. 2242-2249
  • 2
    • 0019887744 scopus 로고
    • Phase separation of integral membrane proteins in Triton X-114 solution
    • Bordier, C. 1981. Phase separation of integral membrane proteins in Triton X-114 solution. J. Biol. Chem. 256: 1604-1607.
    • (1981) J. Biol. Chem. , vol.256 , pp. 1604-1607
    • Bordier, C.1
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of proteins utilizing the principle of protein-dye binding
    • Bradford, M. 1976. A rapid and sensitive method for the quantification of microgram quantities of proteins utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-256.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-256
    • Bradford, M.1
  • 4
    • 0001377673 scopus 로고
    • Mechanism of the oxidation of NADH by quinones. Energetics of one-electron and hydride routes
    • Carlson, B.W. and Miller, L.L. 1985. Mechanism of the oxidation of NADH by quinones. Energetics of one-electron and hydride routes. J. Am. Chem. Soc. 107: 479-485.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 479-485
    • Carlson, B.W.1    Miller, L.L.2
  • 5
    • 0014939358 scopus 로고
    • Physicochemical and kinetic properties of mushroom tyrosinase
    • Duckworth, H.W. and Coleman, J.E. 1970. Physicochemical and kinetic properties of mushroom tyrosinase. J. Biol. Chem. 245: 1613-1625.
    • (1970) J. Biol. Chem. , vol.245 , pp. 1613-1625
    • Duckworth, H.W.1    Coleman, J.E.2
  • 6
    • 0001178114 scopus 로고
    • A spectrophotometric method for the determination of the catecholase activity of tyrosinase and some of its applications
    • El-Bayoumi, M.A. and Frieden, E. 1957. A spectrophotometric method for the determination of the catecholase activity of tyrosinase and some of its applications. J. Am. Chem. Soc. 79: 4854-4858.
    • (1957) J. Am. Chem. Soc. , vol.79 , pp. 4854-4858
    • El-Bayoumi, M.A.1    Frieden, E.2
  • 8
    • 0017359959 scopus 로고
    • A rapid assay for catechol oxidase and laccase using 2-nitro-5-thiobenzoic acid
    • Esterbauer, H., Schwarzl, E., and Hayn, M. 1977. A rapid assay for catechol oxidase and laccase using 2-nitro-5-thiobenzoic acid. Anal. Biochem. 77: 486-494.
    • (1977) Anal. Biochem. , vol.77 , pp. 486-494
    • Esterbauer, H.1    Schwarzl, E.2    Hayn, M.3
  • 9
    • 0018388959 scopus 로고
    • A new spectrophotometric method for the determination of cresolase activity of frog epidermis tyrosinase
    • García-Carmona, F., Pedreño, E., Galindo, J.D., and García-Cánovas, F. 1979. A new spectrophotometric method for the determination of cresolase activity of frog epidermis tyrosinase. Anal Biochem. 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
  • 10
    • 0027440538 scopus 로고
    • New spectrophotometric assay for polyphenol oxidase activity
    • Gauillard, F., Richard-Forget, F., and Nicolas, J. 1993. New spectrophotometric assay for polyphenol oxidase activity. Anal. Biochem. 215: 59-65.
    • (1993) Anal. Biochem. , vol.215 , pp. 59-65
    • Gauillard, F.1    Richard-Forget, F.2    Nicolas, J.3
  • 11
    • 84985161308 scopus 로고
    • Polyphenol oxidase of d'Anjou pears (Pyrus communis L.)
    • Halim, D.H. and Montgomery, M.W. 1978. Polyphenol oxidase of d'Anjou pears (Pyrus communis L.). J. Food Sci. 43: 603-608.
    • (1978) J. Food Sci. , vol.43 , pp. 603-608
    • Halim, D.H.1    Montgomery, M.W.2
  • 12
    • 0024635537 scopus 로고
    • Analysis of mammalian pigmentation at the molecular level
    • Hearing, V.J. and Jiménez, M. 1989. Analysis of mammalian pigmentation at the molecular level. Pigment Cell Research 2: 75-85.
    • (1989) Pigment Cell Research , vol.2 , pp. 75-85
    • Hearing, V.J.1    Jiménez, M.2
  • 14
    • 84955554437 scopus 로고
    • Jandel Scientific (Ed.) Jandel Scientific, Corte Madera, FL
    • Jandel Scientific. 1992. Sigma Plot 5.0. Jandel Scientific (Ed.) Jandel Scientific, Corte Madera, FL.
    • (1992) Sigma Plot 5.0
    • Scientific, J.1
  • 15
    • 0019366638 scopus 로고
    • Quantitative estimation of laccase forms in some white-rot fungi using syringaldazine as a substrate
    • Leonowicz, A. and Grzywnowicz, K. 1981. Quantitative estimation of laccase forms in some white-rot fungi using syringaldazine as a substrate. Enzyme Microbiol. Technol. 3: 55-58.
    • (1981) Enzyme Microbiol. Technol. , vol.3 , pp. 55-58
    • Leonowicz, A.1    Grzywnowicz, K.2
  • 16
    • 0000169232 scopus 로고
    • An algorithm for least-squares estimation of nonlinear parameters
    • Marquardt, D.W. 1963. An algorithm for least-squares estimation of nonlinear parameters. J. Soc. Ind. Appl. Math. 11: 431-441.
    • (1963) J. Soc. Ind. Appl. Math. , vol.11 , pp. 431-441
    • Marquardt, D.W.1
  • 17
    • 0002518418 scopus 로고
    • Chemistry of melanin. Mechanism of oxidation of 3,4- Dihydroxyphenylalanine by tyrosinase
    • Mason, H.S. 1948. Chemistry of melanin. Mechanism of oxidation of 3,4-dihydroxyphenylalanine by tyrosinase. J. Biol. Chem. 172: 83-99.
    • (1948) J. Biol. Chem. , vol.172 , pp. 83-99
    • Mason, H.S.1
  • 18
    • 77049203277 scopus 로고
    • Comparative biochemistry of the phenolase complex
    • Mason, H.S. 1955. Comparative biochemistry of the phenolase complex. Adv. Enzymol. 16: 105-184.
    • (1955) Adv. Enzymol. , vol.16 , pp. 105-184
    • Mason, H.S.1
  • 19
    • 0002797258 scopus 로고
    • Polyphenol oxidase and enzymatic browning of potatoes (Solanum tuberosum) I. Properties of potato polyphenol oxidase
    • Matheis, G. 1987. Polyphenol oxidase and enzymatic browning of potatoes (Solanum tuberosum) I. Properties of potato polyphenol oxidase. Chem. Mikrobiol. Technol. Lebensm. 11: 5-12.
    • (1987) Chem. Mikrobiol. Technol. Lebensm. , vol.11 , pp. 5-12
    • Matheis, G.1
  • 20
    • 77956995750 scopus 로고
    • Food browning as a polyphenol reaction
    • Mathew, A.G. and Parpia, H.A.B. 1971. Food browning as a polyphenol reaction. Adv. Food Res. 19: 75-145.
    • (1971) Adv. Food Res. , vol.19 , pp. 75-145
    • Mathew, A.G.1    Parpia, H.A.B.2
  • 21
    • 46149132278 scopus 로고
    • Polyphenol oxidases in plants. Recent progress
    • Mayer, A.M. 1987. Polyphenol oxidases in plants. Recent progress. Phytochemistry 26: 11-22.
    • (1987) Phytochemistry , vol.26 , pp. 11-22
    • Mayer, A.M.1
  • 23
    • 0013770081 scopus 로고
    • Tyrosine hydroxylation catalyzed by mammalian tyrosinase: An improved method of assay
    • Pomerantz, S.H. 1964. Tyrosine hydroxylation catalyzed by mammalian tyrosinase: an improved method of assay. Biochem. Biophys. Res. Commun. 26: 241-246.
    • (1964) Biochem. Biophys. Res. Commun. , vol.26 , pp. 241-246
    • Pomerantz, S.H.1
  • 24
    • 0001823346 scopus 로고
    • The control of enzymatic browning of fruits
    • H.W. Schultz (Ed.). Avi, New York, NY
    • Ponting, J.D. 1960. The control of enzymatic browning of fruits. In Food Enzymes. H.W. Schultz (Ed.). Avi, New York, NY.
    • (1960) Food Enzymes
    • Ponting, J.D.1
  • 25
    • 0023690603 scopus 로고
    • Progress in the chemistry of melanins and related metabolites
    • Prota, G. 1988. Progress in the chemistry of melanins and related metabolites. Med. Res. Rev. 8: 525-556.
    • (1988) Med. Res. Rev. , vol.8 , pp. 525-556
    • Prota, G.1
  • 26
    • 0000553862 scopus 로고
    • Purification and some properties of two polyphenol oxidases from Bartlett pears
    • Rivas, N.J. and Whitaker, J.N. 1973. Purification and some properties of two polyphenol oxidases from Bartlett pears. Plant Physiol. 52: 501-507.
    • (1973) Plant Physiol. , vol.52 , pp. 501-507
    • Rivas, N.J.1    Whitaker, J.N.2
  • 27
    • 85053591293 scopus 로고
    • Tyrosinase
    • R. Lontie (Ed.), CRC Press, Boca Ratón, FL
    • Robb, D.A. 1984. Tyrosinase. Vol II in Copper Proteins Copper Enzymes, R. Lontie (Ed.), p. 207-240. CRC Press, Boca Ratón, FL.
    • (1984) Copper Proteins Copper Enzymes , vol.2 , pp. 207-240
    • Robb, D.A.1
  • 29
    • 0028140296 scopus 로고
    • A continuous spectrophotometric method for the determination of monophenolase activity of tyrosinase using 3-methyl-2-benzothiazolinone hydrazone
    • Rodríguez-López, J.N., Escribano, J., and García-Cánovas, F. 1994. A continuous spectrophotometric method for the determination of monophenolase activity of tyrosinase using 3-methyl-2-benzothiazolinone hydrazone. Anal. Biochem. 216: 205-212.
    • (1994) Anal. Biochem. , vol.216 , pp. 205-212
    • Rodríguez-López, J.N.1    Escribano, J.2    García-Cánovas, F.3
  • 30
    • 0024342694 scopus 로고
    • A chromogenic assay for catecholoxidases based on the addition of L-proline to quinones
    • Rzepecki, L.M. and Waite, J.H. 1989. A chromogenic assay for catecholoxidases based on the addition of L-proline to quinones. Anal. Biochem. 179: 375-381.
    • (1989) Anal. Biochem. , vol.179 , pp. 375-381
    • Rzepecki, L.M.1    Waite, J.H.2
  • 31
    • 0000458402 scopus 로고
    • Novel procedure for extraction of a latent grape polyphenol oxidase using temperature-induced phase separation in Triton X-114
    • Sánchez-Ferrer, A., Bru, R., and García-Carmona, F. 1989. Novel procedure for extraction of a latent grape polyphenol oxidase using temperature-induced phase separation in Triton X-114. Plant Physiol. 91: 1481-1487.
    • (1989) Plant Physiol. , vol.91 , pp. 1481-1487
    • Sánchez-Ferrer, A.1    Bru, R.2    García-Carmona, F.3
  • 32
    • 4243998280 scopus 로고
    • Partial purification of soluble potato polyphenol oxidase by partitioning in an aqueous two-phase system
    • Sánchez-Ferrer, A., Laveda, F., and García-Carmona, F. 1993. Partial purification of soluble potato polyphenol oxidase by partitioning in an aqueous two-phase system. J. Agric. Food Chem. 41: 1219-1224.
    • (1993) J. Agric. Food Chem. , vol.41 , pp. 1219-1224
    • Sánchez-Ferrer, A.1    Laveda, F.2    García-Carmona, F.3
  • 34
    • 0023444834 scopus 로고
    • A chromogenic oxidative coupling reaction of laccase: Applications for laccase and angiotensin I converting enzyme assay
    • Shin, T., Murao, S., and Matsumura, E. 1987. A chromogenic oxidative coupling reaction of laccase: applications for laccase and angiotensin I converting enzyme assay. Anal. Biochem. 116: 380-388.
    • (1987) Anal. Biochem. , vol.116 , pp. 380-388
    • Shin, T.1    Murao, S.2    Matsumura, E.3
  • 35
    • 84986528073 scopus 로고
    • Characterization and inhibition of polyphenol oxidase from pears (Pyrus communis L. cv. Bosc and Red)
    • Siddiq, M., Cash, J.N., Sinha, N.K., and Akhter, P. 1994. Characterization and inhibition of polyphenol oxidase from pears (Pyrus communis L. cv. Bosc and Red), J. Food Biochemistry 17: 327-337.
    • (1994) J. Food Biochemistry , vol.17 , pp. 327-337
    • Siddiq, M.1    Cash, J.N.2    Sinha, N.K.3    Akhter, P.4
  • 36
    • 0000894326 scopus 로고
    • Improved methods for the extraction of polyphenol oxidase from d'Anjou pears
    • Smith, D.M. and Montgomery, M.W. 1985. Improved methods for the extraction of polyphenol oxidase from d'Anjou pears. Phytochemistry 24: 901-904.
    • (1985) Phytochemistry , vol.24 , pp. 901-904
    • Smith, D.M.1    Montgomery, M.W.2
  • 37
    • 0001313055 scopus 로고
    • Polyphenol oxidase in Bartlett pears
    • Tate, J.N., Luh, B.S., and York, G.K. 1964. Polyphenol oxidase in Bartlett pears. J. Food Sci. 29: 829-836.
    • (1964) J. Food Sci. , vol.29 , pp. 829-836
    • Tate, J.N.1    Luh, B.S.2    York, G.K.3
  • 38
    • 0022057370 scopus 로고
    • A spectrophotometric assay for mammalian tyrosinase utilizing the formation of melanochrome from L-dopa
    • Vachtenheim, J., Duchon, J., and Matous, B. 1985. A spectrophotometric assay for mammalian tyrosinase utilizing the formation of melanochrome from L-dopa. Anal. Biochem. 146: 405-410.
    • (1985) Anal. Biochem. , vol.146 , pp. 405-410
    • Vachtenheim, J.1    Duchon, J.2    Matous, B.3
  • 39
    • 0019741905 scopus 로고
    • Polyphenol oxidase and peroxidase in fruits and vegetables
    • Vamos-Vigyázó, L. 1981. Polyphenol oxidase and peroxidase in fruits and vegetables. CRC Crit. Rev. Food Sci. Nutr. 15: 49-127.
    • (1981) CRC Crit. Rev. Food Sci. Nutr. , vol.15 , pp. 49-127
    • Vamos-Vigyázó, L.1
  • 40
    • 0017191181 scopus 로고
    • Calculating extinction coefficients for enzymatically produced o-quinones
    • Waite, J.H. 1976. Calculating extinction coefficients for enzymatically produced o-quinones. Anal. Biochem. 75: 211-218.
    • (1976) Anal. Biochem. , vol.75 , pp. 211-218
    • Waite, J.H.1
  • 41
    • 0000194252 scopus 로고
    • Mechanism of oxidoreductase important in food component modification
    • T. Richardson, and J.W. Finley (Ed.), Avi, New York, NY
    • Whitaker, J.R. 1985. Mechanism of oxidoreductase important in food component modification. In Chemical Changes in Food Processing. T. Richardson, and J.W. Finley (Ed.), p. 121-176. Avi, New York, NY.
    • (1985) Chemical Changes in Food Processing , pp. 121-176
    • Whitaker, J.R.1
  • 42
    • 0005499841 scopus 로고
    • Statistical estimations in enzyme kinetics
    • Wilkinson, G.N. 1961. Statistical estimations in enzyme kinetics. Biochem. J. 80: 324-332.
    • (1961) Biochem. J. , vol.80 , pp. 324-332
    • Wilkinson, G.N.1
  • 43
    • 0025910929 scopus 로고
    • New assays for the tyrosine hydroxylase and dopa oxidase activities of tyrosinase
    • Winder, A.J. and Harris, H. 1991. New assays for the tyrosine hydroxylase and dopa oxidase activities of tyrosinase. Eur. J. Biochem. 198: 317-326.
    • (1991) Eur. J. Biochem. , vol.198 , pp. 317-326
    • Winder, A.J.1    Harris, H.2
  • 44
    • 0001121260 scopus 로고
    • Purificaton of d'Anjou pear (Pyrus communis L.) polyphenol oxidase
    • Wissemann, K.W. and Montgomery, M.W. 1985. Purificaton of d'Anjou pear (Pyrus communis L.) polyphenol oxidase. Plant Physiol. 78: 256-262.
    • (1985) Plant Physiol. , vol.78 , pp. 256-262
    • Wissemann, K.W.1    Montgomery, M.W.2
  • 45
    • 84986734258 scopus 로고
    • Polyphenol oxidase from Yali pear (Pyrus bretschneideri)
    • Zhou, H. and Feng, X. 1991. Polyphenol oxidase from Yali pear (Pyrus bretschneideri). J. Sci. Food Agric. 57: 307-313.
    • (1991) J. Sci. Food Agric. , vol.57 , pp. 307-313
    • Zhou, H.1    Feng, X.2


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