Mechanisms of Oxidoreductases Important in Food Component Modification

  • John R. Whitaker
Chapter
Part of the Basic Symposium Series book series (IFTBSS)

Abstract

Six types of chemical reactions are catalyzed by enzymes; these are oxidoreduction, transfer, hydrolysis, making or adding to double bonds (lyases), isomerization, and bond formation requiring high-energy phosphates (ligases). While all of these reactions are important in food production, the food scientist is especially concerned with oxidoreduction and hydrolysis reactions. In general, much more emphasis is placed on the hydrolytic reactions than on the oxidoreductions, perhaps because hydrolytic reactions are so important in malting and brewing, in cheese production, in conversion of starch to glucose and fructose, and in human metabolism.

Keywords

Uric Acid Xanthine Oxidase Alcohol Dehydrogenase Glucose Oxidase Aldehyde Dehydrogenase 
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References

  1. ALLEN, J.C. 1968. Soybean lipoxygenase. I. Purification, and the effect of organic solvents upon the kinetics of the reaction. Eur. J. Biochem. 4, 201–208.CrossRefGoogle Scholar
  2. AOSHIMA, H., KAJIWARA, T., and HATANAKA, A. 1981. Decomposition of lipid hydroperoxide by soybean lipoxygenase-1 under aerobic conditions studied by high performance liquid chromatography and the spin trapping method. Agric. Biol. Chem. 45, 2245–2251.CrossRefGoogle Scholar
  3. ARGOS, P., GARAVITO, M., EVENTOFF, W., and ROSSMAN, M.G. 1978. Simi-larities in active center geometries of zinc-containing enzymes, proteases and dehydrogenases. J. Mol. Biol. 126, 141–158.CrossRefGoogle Scholar
  4. BACKLIN, K. 1958. The equilibrium constant of the system ethanol, aldehyde, DPN+, DPNH and H+. Acta Chem. Scand. 12, 1279–1285.CrossRefGoogle Scholar
  5. BARBER, M.J., and SIEGEL, L.M. 1983. Electron paramagnetic resonance and Potentiometrie studies of arsenite interaction with the molybdenum centers of xanthine oxidase, xanthine dehydrogenase and aldehyde oxidase: A specific stabilization of the molybdenum (V) oxidation state. Biochemistry 22, 618–624.CrossRefGoogle Scholar
  6. BARBER, M.J., BRAY, R.C., CAMMACK, R., and COUGHLAN, M.P. 1977. Oxidation-reduction potentials for turkey liver xanthine dehydrogenase and the origins of oxidase and dehydrogenase behavior in molybdenum-containing hydroxylases. Biochem. J. 163, 279–289.Google Scholar
  7. BARBER, M.J., COUGHLAN, M.P., RAJAGOPALAN, K.V., and SIEGEL, L.M. 1982. Rabbit liver aldehyde oxidase: Reduction potentials and spectroscopic properties. In Flavins and Flavoproteins. V. Massey and C.H. Williams (Editors), pp. 805 – 809. Elsevier/North-Holland, Amsterdam.Google Scholar
  8. BOOTH, V.H. 1938. The specificity of xanthine oxidase. Biochem. J. 32, 494–502.Google Scholar
  9. BOUCHILLOUX, S., McMAHILL, P., and MASON, H.S. 1963. Multiple forms of mushroom tyrosinase. Purification and molecular properties of the enzymes. J. Biol. Chem. 238, 1699–1707.Google Scholar
  10. BRANDEN, C. -I. 1977. Mechanism of action of liver alcohol dehydrogenase. In Alcohol and Aldehyde Metabolism Systems. R.G Thurman, J.R. Williamson, H.R. Drott, and B. Chance (Editors), Vol. 2, pp. 17–32. Academic Press, NY.Google Scholar
  11. BRANDEN, C.-I., JORNVALL, H, EKLUND, H., and FURUGREN, B. 1975. Alcohol dehydrogenases. In The Enzymes. P.D. Boyer (Editor), 3rd Edition, Vol. 11, pp. 103–190. Academic Press, NY.Google Scholar
  12. BRAY, R.C. 1976. Molybdenum iron-sulfur flavin hydroxylases and related enzymes. In The Enzymes. P.D. Boyer (Editor), 3rd Edition, Vol. 12, pp. 299–419. Academic Press, NY.Google Scholar
  13. BRAY, R.C. 1982. The flavin and the other catalytic and redox centers of xanthine oxidase and related enzymes. In Flavins and Flavoproteins. V. Massey and C.H. Williams (Editors), pp. 775–785. Elsevier/North-Holland, Amsterdam.Google Scholar
  14. BRAY, R.C., PALMER, G., and BEINERT, H. 1964. The electron transfer sequence in xanthine oxidase by electron paramagnetic resonance spectroscopy. II. Kinetic studies employing rapid freezing. J. Biol. Chem. 239, 2667–2676.Google Scholar
  15. BRIGHT, H.J., and APPLEBY, M. 1969. pH dependence of the individual steps in the glucose oxidase reaction. J. Biol. Chem. 244 3625–3634.Google Scholar
  16. BRIGHT, H.J., and PORTER, D.J.T. 1976. Flavoprotein oxidases. In The Enzymes. P.D. Boyer (Editor), 3rd Edition, Vol. 12, pp. 421–505. Academic Press, NY.Google Scholar
  17. BUCKLEY, P.D., and DUNN, M.F. 1982. Observation of acyl-enzyme intermedi-ates in the sheep liver aldehyde dehydrogenase catalytic mechanism via rapid- scanning UV-visible spectroscopy. Prog. Clin. Biol. Res. 114, 23–35.Google Scholar
  18. BUCKLEY, P.D., BENNETT, A.F., and BLACKWELL, L.F. 1982. A general mechanism for the action of cytoplasmic sheep liver aldehyde dehydrogenase based on the results of proton burst studies. Prog. Clin, Biol. Res. 114, 53–60.Google Scholar
  19. CEROVSKA, N., and LEBLOVA, S. 1981. Kinetics of reaction catalyzed by pea al-cohol dehydrogenase. Biochem. Physiol. Pflanz. 176, 157–162.Google Scholar
  20. CHAN, H.W.-S. 1973. Soya-bean lipoxygenase: An iron-containing dioxygenase. Biochim. Biophys. Acta 327, 32–35.Google Scholar
  21. CHAN, T.W., and BRUICE, T.C. 1977. One and two electron transfer reactions of glucose oxidase. J. Am. Chem. Soc. 99, 2387–2389.CrossRefGoogle Scholar
  22. CHEN, A.S.-M.O. 1984. Purification and characterization of pea lipoxygenases; re-lationship to quality deterioration in frozen peas. Ph.D. Dissertation, Univ. of California, Davis.Google Scholar
  23. CHIBA, H., SASAKI, R., YOSHIKAWA, M., TAKAHASHI, N., SUGIMOTO, E., and SUMEJIMA, H. 1979. Soybean deodorization with aldehyde oxidase. Jpn. Kokai Tokkyo Koho 79 32, 644.Google Scholar
  24. CLELAND, W.W. 1963A. The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations. Biochim. Biophys. Acta 67, 104–107.Google Scholar
  25. CLELAND, W.W. 1963B. The kinetics of enzyme-catalyzed reactions with two or more substrates or products. II. Inhibition-nomenclature and theory. Biochim. Biophys. Acta 67, 173–187.Google Scholar
  26. CLELAND, W.W. 1963C. The kinetics of enzyme-catalyzed reactions with two or more substrates or products. III. Prediction of initial velocity and inhibition patterns by inspection. Biochim. Biophys. Acta 67, 188–196.Google Scholar
  27. CLIFFORD, A.J., HO, C, and SWENERTON, H. 1983. Homogenized bovine milk xanthine oxidase: A critique of the hypothesis relating to plasmalogen depletion and cardiovascular disease. Am. J. Clin. Nutr. 38, 327–332.Google Scholar
  28. COUGHLAN, M.P., and RAJAGOPALAN, K.V. 1980. The kinetic mechanism of xanthine dehydrogenase and related enzymes. Eur. J. Biochem. 105, 81 – 84.CrossRefGoogle Scholar
  29. CROW, K.E., KITSON, T.M., MACGIBBON, A.K.H., and BATT, R.D. 1974. Intracellular localization and properties of aldehyde dehydrogenase from sheep liver. Biochim. Biophys. Acta 350, 121–128.Google Scholar
  30. DE GROOT, J.J.M.C., VELDINK, G.A., VLIEGENTHART, J.F.G., BOLDINGH, J., WEVER, R., and VAN GELDER, B.F. 1975. Demonstration by EPR spectroscopy of the functional role of iron in soybean 1-lipoxygenase. Biochim. Biophys. Acta 377, 71–79.Google Scholar
  31. DEINUM, J., LERCH, K., and REINHAMMER, B. 1976. An EPR study of Neuro- spora tyrosinase. FEBS Lett. 69, 161–164.CrossRefGoogle Scholar
  32. DIXON, M., and WEBB, E.C. 1958. Enzymes, 1st Edition. Longmans, Green, NY.Google Scholar
  33. DUNFORD, H.B. 1982. Peroxidase. Adv. Inorg. Biochem. 4, 41–68.Google Scholar
  34. DUNFORD, H.B., and ARAISO, T. 1979. Horseradish peroxidase. XXXVI. On the difference between peroxidase and metmyoglobin. Biochem. Biophys. Res. Commun. 89, 764–768.CrossRefGoogle Scholar
  35. DWORSCHACK, R.T., and PLAPP, B.V. 1977. Kinetics of native and activated isozymes of horse liver alcohol dehydrogenase. Biochemistry 18, 111–116.CrossRefGoogle Scholar
  36. ECKFELDT, J.H., and YONETANI, T. 1976. Kinetics and mechanism of the F1 iso¬zyme of horse liver aldehyde dehydrogenase. Arch. Biochem. Biophys. 173, 273–281.CrossRefGoogle Scholar
  37. EGMOND, M., VLIEGENTHART, J, and BOLDINGH, J. 1972. Stereospecificity of the hydrogen abstraction at carbon atom n-8 in the oxygenation of linoleic acid by lipoxygenases from corn germs and soybeans. Biochem. Biophys. Res. Commun. 48, 1055–1060.CrossRefGoogle Scholar
  38. EKLUND, H., NORDSTROM, B., ZEPPEZAUER, E., SODERLUND, G., OHLSSON, I., BOIWE, T., SODERBERG, B.-O., TAPIA, O., BRANDEN, C.-I., and AKESON, A. 1976. Three-dimensional structure of horse liver alcohol dehydrogenase at 2.4 A resolution. J. Mol. Biol. 102, 27–59.CrossRefGoogle Scholar
  39. ESKIN, N.A.M., GROSSMAN, S., and PINSKY, A. 1977. Biochemistry of lipoxygenase in relation to food quality. CRC Crit. Rev. Food Sci. Nutr. 9, 1–40.Google Scholar
  40. FELDMAN, R.I., and WEINER, H. 1972. Horse liver aldehyde dehydrogenase. II. Kinetics and mechanistic implications of the dehydrogenase and esterase activity. J. Biol. Chem. 247, 267–272.Google Scholar
  41. FRY, D.C., and STROTHKAMP, K.G. 1983. Photooxidation oiAgaricus bisporus tyrosinase: Modification of the binuclear site. Biochemistry 22, 4949–4953.CrossRefGoogle Scholar
  42. GALLIARD, T. 1975. Degradation of plant lipids by hydrolytic and oxidative enzymes. In Advances in the Chemistry and Biochemistry of Plant Lipids. T. Galliard and E.I. Mercet (Editors). Academic Press, NY.Google Scholar
  43. GALLIARD, T., and PHILLIPS, D. 1971. Lipoxygenase from potato tubers. Partial purification and properties of an enzyme that specifically oxygenates the 9-position of linoleic acid. Biochem. J. 124, 431–488.Google Scholar
  44. GARDNER, H., and WEISLEDER, D. 1970. Lipoxygenase from Zea mays: 9-D- hydroperoxy-¿rcms-10, cis-12-octadecadienoic acid from linoleic acid. Lipids 5, 678–683.CrossRefGoogle Scholar
  45. GIBIAN, M.J., and GALA WAY, R.A. 1977. Chemical aspects of lipoxygenase reac-tions. In Bioorganic Chemistry. E.E. Van Tamelen (Editor), Vol. 1, pp. 117–136. Academic Press, NY.Google Scholar
  46. GIBSON, Q.H., SWOBODA, B.E.P., and MASSEY, V. 1964. Kinetics and mechanism of action of glucose oxidase. J. Biol. Chem. 239, 3927-3934.Google Scholar
  47. GOLAN-GOLDHIRSH, A., and WHITAKER, J.R. 1984A. Relation between structure of polyphenol oxidase and prevention of browning. Adv. Exp. Med. Biol. 177, 437–456.Google Scholar
  48. GOLAN-GOLDHIRSH, A., and WHITAKER, J.R. 1984B. Unpublished data.Google Scholar
  49. GOLAN-GOLDHIRSH, A., and WHITAKER, J.R. 1984C. Effect of ascorbic acid, sodium bisulfite and thiol compounds on mushroom on polyphenol oxidase. J. Agric. Food. Chem. 32, 1003–1009.Google Scholar
  50. GREEVES, M.A., and FINK, A.L. 1980. The binding of NADH to horse liver alcohol dehydrogenase at subzero temperatures: A three step reaction. J. Biol. Chem. 255, 3248–3250.Google Scholar
  51. GUTFREUND, H., and STURTEVANT, J.M. 1959. Steps in the oxidation of xanthine to uric acid catalyzed by milk xanthine oxidase. Biochem. J. 73, 1–6.Google Scholar
  52. HAINING, J.L., and AXELROD, B. 1958. Induction period in the lipoxygenase- catalyzed oxidation of linoleic acid and its abolition by substrate peroxide. J. Biol. Chem. 232, 193–202.Google Scholar
  53. HAMBERG, M., and SAMUELSSON, B. 1967. On the specificity of the oxygenation of unsaturated fatty acids catalyzed by soybean lipoxidase. J. Biol. Chem. 242, 5329–5335.Google Scholar
  54. HANSON, L.K., CHANG, C.K., DAVIS, M.J., and FAJER, J. 1981. Electron path-ways in catalase and peroxidase enzymic catalysis. Metal and macrocycle oxidations of iron porphyrins and chlorins. J. Am. Chem. Soc. 103, 663–670.CrossRefGoogle Scholar
  55. HART, G.J., and DICKINSON, F.M. 1978. Kinetic properties of aldehyde dehydro¬genase from sheep liver mitochondria. Biochem. J. 175, 899–908.Google Scholar
  56. HART, L.I., McGARTOLL, M.A., CHAPMAN, H.R., and BRAY, R.C. 1970. Composition of milk xanthine oxidase. Biochem. J. 116, 851–864.Google Scholar
  57. HEMMERICH, P., and MASSEY, V. 1981. The role of apoprotein in directing pathways of flavin catalysis. In Oxidases and Related Redox Systems. T.E. King, H.S. Mason, and M. Morrison (Editors), pp. 379–405. Pergamon Press, Oxford.Google Scholar
  58. HIMMELWRIGHT, R.S., EICKMAN, N.C., LuBIEN, C.D., LERCH, K., and SOLOMON, E.I. 1980. Chemical and spectroscopic studies of the binuclear copper active site of Neurospora tyrosinase: Comparison to hemocyanins. J. Am. Chem. Soc 102, 7339–7344.Google Scholar
  59. HOLMAN, R.T. 1947. Crystalline lipoxidase. II. Lipoxidase activity. Arch. Biochem. 15, 403–413.Google Scholar
  60. INGRAHAM, L.L. 1957. Variation of the Michaelis constant in polyphenol oxidase catalyzed oxidations: Substrate structure and concentration. J. Am. Chem. Soc. 79, 666–669.CrossRefGoogle Scholar
  61. JACOB, G.S., and ORME-JOHNSON, W.H. 1979A. Catalase of Neurospora crassa. 1. Induction, purification and physical properties. Biochemistry 18, 2967–2975.Google Scholar
  62. JACOB, G.S., and ORME-JOHNSON, W.H. 1979B. Catalase of Neurospora crassa. 2. Electron paramagnetic resonance and chemical properties of the prosthetic group. Biochemistry 42, 2975–2980.Google Scholar
  63. KEILIN, D., and HARTREE, E.F. 1948. Properties of glucose oxidase (notatin). Biochem. J. 42, 221–229.Google Scholar
  64. KEILIN, D., and NICHOLLS, P. 1958. Reactions of catalase with hydrogen peroxide and hydrogen donors. Biochim. Biophys. Acta 29, 302–307.CrossRefGoogle Scholar
  65. LERCH, K. 1976. Neurospora tyrosinase: Molecular weight copper content and spectral properties. FEBS Lett. 69, 157–160.CrossRefGoogle Scholar
  66. LERCH, K. 1978. Amino acid sequence of tyrosinase from Neurospora crassa. Proc. Natl. Acad. Sei. U.S.A. 75, 3635–3639.CrossRefGoogle Scholar
  67. LERNER, A.B. 1953. Metabolism of phenylalanine and tyrosine. Adv. Enzymol. 14, 49–77.Google Scholar
  68. MacGIBBON, A.K.H., BLACKWELL, L.F., and BUCKLEY, P.D. 1977A. Kinetics of sheep-liver cytoplasmic aldehyde dehydrogenase. Eur. J. Biochem. 77, 93–100.Google Scholar
  69. MacGIBBON, A.K.H., BLACKWELL, L.F., and BUCKLEY, P.D. 1977B. Pre-steady-state kinetic studies on cytoplasmic sheep liver aldehyde dehydrogenase. Biochem. J. 167, 469–477.Google Scholar
  70. MACRAE, A.R., and DUGGLEBY, R.G. 1968. Substrates and inhibitors of potato tuber phenolase. Phytochemistry 7, 855–861.CrossRefGoogle Scholar
  71. MALMSTRÖM, B.G. 1982. Enzymology of oxygen. Annu. Rev. Biochem. 51, 21–59.CrossRefGoogle Scholar
  72. MASSEY, V., BRUMBY, P.E., KOMAI, H., and PALMER, G. 1969. Milk xanthine oxidase. Some spectral and kinetic properties. J. Biol. Chem. 244, 1682–1691.Google Scholar
  73. MORELL, D.B. 1952. Natural and catalytic activities of milk xanthine oxidase. Biochem. J. 51, 657–666.Google Scholar
  74. MORISHIMA, I., and OGAWA, S. 1978. Proton nuclear magnetic resonance studies of compounds I and II of horseradish peroxidase. Biochem. Biophys. Res. Commun. 83, 946–953.CrossRefGoogle Scholar
  75. MÜLLER, D. 1928. Studien über ein neues Enzym Glykoseoxydase. I. Biochem. Z. 199, 136–170.Google Scholar
  76. NAKAMURA, S., and YAMAZAKI, I. 1969. One-electron transfer reactions in bio-chemical systems. IV. Mixed mechanism in the reaction of milk xanthine oxidase with electron acceptors. Biochim. Biophys. Acta 189, 29–37.CrossRefGoogle Scholar
  77. NASON, A., LEE, K.-Y., PAN, S.-S., KETCHUM, P.A., LAMBERTI, A., and DE VRIES, J. 1971. In vitro formation of assimilatory reduced nicotinamide adenine di- nucleotide phosphate:nitrate reductase from a Neurospora mutant and a component of molybdenum enzymes. Proc. Natl. Acad. Sei U.S.A. 68, 3242–3246.CrossRefGoogle Scholar
  78. OLSON, J.S., BALLOU, D.P., PALMER, G., and MASSEY, V. 1974A. Mechanism of action of xanthine oxidase. J. Biol. Chem. 249, 4363–4382.Google Scholar
  79. OLSON, J.S., BALLOU, D.P., PALMER, G., and MASSEY, V. 1974B. Reaction of xanthine oxidase with molecular oxygen. J. Biol. Chem. 249, 4350–4362.Google Scholar
  80. OSTER, K.A., and ROSS, D.J. 1983. The XO factor: And how it can destroy your arteries, your heart, your life! As told to Hazel H. Richmond Dawkins. N. Sampsidi and M.D. Morrison (Editors). Parks City Press, NY.Google Scholar
  81. PAZUR, J.H., and KLEPPE, K. 1964. The oxidation of glucose and related com-pounds by glucose oxidase from Aspergillus niger. Biochemistry 3, 578–583.CrossRefGoogle Scholar
  82. PFIFFNER, E., DIETLER, C., and LERCH, K. 1981. Coordination of the active site copper in Neurospora tyrosinase. In Invertebrate Oxygen-Binding Proteins: Structure, Active Site, and Function. J. Lamy and J. Lamy, (Editors), pp. 541–551. Marcel Dekker, NY.Google Scholar
  83. PISTORIUS, E.K., and AXELROD, B. 1973. Ferric iron as a cofactor of lipoxygenase. Fed. Proc., Fed. Am. Soc. Exp. Biol. 32, 544.Google Scholar
  84. PISTORIUS, E.K., AXELROD, B., and PALMER, G. 1976. Evidence for participation of iron in lipoxygenase reactions from optical and electron spin resonance studies. J. Biol. Chem. 251, 7144–7148.Google Scholar
  85. PORTER, D.J.T., VOET, J.G., and BRIGHT, H.J. 1972. Nitroalkanes as reductive substrates for flavoprotein oxidases. Z. Naturforsch., B: Anorg. Chem., Org. Chem., Biochem., Biophys., Biol. 27, 1052–1053.Google Scholar
  86. RIVAS, N.J., and WHITAKER, J.R. 1973. Purification and some properties of two polyphenol oxidases from Bartlett pears. Plant Physiol. 52, 501–507.CrossRefGoogle Scholar
  87. ROBB, D.A., SWAIN, T., and MAPSON, L.W. 1966. Substrates and inhibitors of the activated tyrosinase of broad bean (Vicia faba). Phytochemistry 5, 665–675.CrossRefGoogle Scholar
  88. ROZA, M., and FRANCKE, A. 1973. Soybean lipoxygenase. Iron-containing enzyme. Biochim. Biophys. Acta 327, 24–31.Google Scholar
  89. SCHWIMMER, S. 1982. Source Book for Food Enzymology. Avi Publishing Co., Westport, CT.Google Scholar
  90. SIDDIQI, A.M., and TAPPEL, A.L. 1957. Comparison of some lipoxidases and their mechanism of action. J. Am. Oil Chem. Soc. 34, 529–533.CrossRefGoogle Scholar
  91. SIDHU, R.S., and TAPPEL, A.L. 1957A. Human liver aldehyde dehydrogenase. Esterase activity. J. Biol. Chem. 250, 7894–7898.Google Scholar
  92. SIDHU, R.S., and TAPPEL, A.L. 1957B. Human liver aldehyde dehydrogenase. Kinetics of aldehyde oxidation. J. Biol. Chem. 250, 7899–7904.Google Scholar
  93. SPIRO, T.G., STRONG, J.D., and STEIN, P. 1979. Porphyrin core expansion and doming in heme proteins. New evidence from resonance Raman spectra of six- coordinate high-spin iron(III) hemes. J. Am. Chem. Soc. 101, 2648–2655.CrossRefGoogle Scholar
  94. STIBOROVA, M., and LEBLOVA, S. 1979. Kinetics of the reaction catalyzed by rape alcohol dehydrogenase. Phytochemistry 18, 23–24.CrossRefGoogle Scholar
  95. STROTHER, G.K., and ACKERMAN, E. 1961. Physical factors influencing catalase rate constants. Biochim. Biophys. Acta 47, 317–326.CrossRefGoogle Scholar
  96. STROTHKAMP, K.G., JOLLEY, R.L., JR., and MASON, H.S. 1976. Quaternary structure of mushroom tyrosinase. Biochem. Biophys. Res. Commun. 70, 519–524.CrossRefGoogle Scholar
  97. SUMNER, J.B., and DOUNCE, A.L. 1937. Crystalline catalase. J. Biol. Chem. 121, 417–424.Google Scholar
  98. SUND, H., and THEORELL, H. 1963. Alcohol dehydrogenases. In The Enzymes. P.D. Boyer, H. Lardy, and K. Myrback (Editors), 2nd Revised Edition, Vol. 7, pp. 25–83. Academic Press, NY.Google Scholar
  99. TAKAHASHI, N., SASAKI, R., and CHIBA, H. 1979. Enzymic improvement of food flavor. IV Oxidation of aldehydes in soybean extracts by aldehyde oxidase. Agric. Biol. Chem 43, 2557–2561.CrossRefGoogle Scholar
  100. TAPPEL, A.L., BOYER, P.D., and LUNDBERG, W.O. 1952. The reaction mecha-nism of soybean lipoxidase. J. Biol Chem. 199, 267–281.Google Scholar
  101. THEORELL, H., HOLMAN, R.T., and AKESON, A. 1947. Crystalline lipoxidase. Acta Chem. Scand. 1, 571–576.CrossRefGoogle Scholar
  102. TSAI, C.S., and SHER, D.S. 1980. Multifunctionality of liver alcohol dehydrogenase. Studies of aldehyde dehydrogenase activity. Arch. Biochem. Biophys. 199, 626–634.CrossRefGoogle Scholar
  103. VERHAGEN, J., VELDINK, G.A., EGMOND, M.R., VLIEGENTHART, J.F.G., BOLDINGH, J., VAN DER STAR, J. 1978. Steady-state kinetics of the anaerobic re-action of soybean lipoxygenase-1 with linoleic acid and 13-L-hydroperoxylinoleic acid. Biochim. Biophys. Acta 529, 369–379.Google Scholar
  104. VLIEGENTHART, J.F.G., VELDINK, G.A., and BOLDINGH, J. 1979. Recent prog-ress in the study on the mechanism of action of soybean lipoxygenase. J. Agric. Food Chem. 27, 623–626.CrossRefGoogle Scholar
  105. WELINDER, K.G. 1976. Covalent structure of the glycoprotein horseradish peroxidase (EC 1.11.1.7). FEBS Lett. 72, 19–23.CrossRefGoogle Scholar
  106. WELINDER, K.G. 1979. Amino acid sequence studies of horseradish peroxidase. 4. Amino and carboxyl termini, cyanogen bromide and tryptic fragments, the complete sequence, and some structural characteristics of horseradish peroxidase C. Eur. J. Biochem. 96, 483–502.CrossRefGoogle Scholar
  107. WHITAKER, J.R. 1972. Principles of Enzymology for the Food Sciences. Marcel Dekker, NY.Google Scholar
  108. WINKLER, M.E., LERCH, K., and SOLOMON, E.I. 1981. Competitive inhibitor binding to the binuclear copper active site in tyrosinase. J. Am. Chem. Soc. 103, 7001–7003.CrossRefGoogle Scholar
  109. WONG, T.C., LUH, B.S., and WHITAKER, J.R. 1971. Isolation and characterization of polyphenol oxidase isozymes of clingstone peach. Plant Physiol. 48, 19–23.CrossRefGoogle Scholar
  110. WOOD, B.J.B., and INGRAHAM, L.L. 1965. Labelled tyrosinase from labelled sub-strate. Nature (London) 205, 291–292.CrossRefGoogle Scholar

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© AVI Publishing Co. 1985

Authors and Affiliations

  • John R. Whitaker
    • 1
  1. 1.Department of Food Science and TechnologyUniversity of CaliforniaDavisUSA

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