Abstract
The variety of chemical transformations catalyzed by enzymes make these catalysts a prime target for exploitation by the emerging biotechnology industries. Over the last two decades, intense research in the area of enzyme technology has provided many approaches that facilitate the practical application of enzymes. This review focuses on oxidoreductases, the large class of enzymes catalyzing biological oxidation/reduction reactions. Since so much industrial chemistry involves oxidation/reduction processes, the use of oxidoreductases to carry out synthetic transformations is a major area of interest. Of particular significance in this regard are oxidoreductase–mediated asymmetric syntheses of amino acids, steroids, and other pharmaceuticals, and of a host of specialty chemicals. Another area of major importance is the current extensive use of oxidoreductases in clinical diagnosis and other analytical applications. Future applications for oxidoreductases can be visualized in areas as diverse as polymer synthesis, pollution control, and oxygenation of hydrocarbons.
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References
Dixon, M. and Webb, E.C. 1979. p. 11. Enzymes. Academic Press, New York.
Homandberg, G.A. and Laskowski, M., Jr. 1979. Enzymatic resynthesis of the hydrolyzed peptide bond(s) in ribonuclease S. Biochemistry 18: 586–592.
Fink, A.L. and Cartwright, S.J. 1981. Cryoenzymology, p. 145–207. In CRC Critical Reviews in Biochemistry.
May, S.W. and Li, N.N. 1977. Liquid-Membrane Encapsulated Enzymes, p. 171–190. In Biomedical Applications of Immobilized Enzymes and Proteins. Vol. 1. T.M.S. Chang (ed.), Plenum Press, New York.
Klibanov, A.M. 1983. Immobilized enzymes as practical catalysts. Science 219: 722–727.
Godfrey, T. and Rerchelt, J. 1983. Industrial Enzymology. The Nature Press, New York.
Zaborsky, O.R. 1973. Immobilized Enzymes. CRC Press, Cleveland, Ohio.
Mosbach, K. (ed.), 1976. Immobilized Enzymes. In Methods Enzymol. 44. Academic Press, New York.
Chibata, I. (ed.), 1978. Immobilized Enzymes in Research and Development. John Wiley and Sons, New York.
Wingard, L.B., Jr., Katchalski-Katzir, E., and Goldstein, L. (eds.), 1976. Immobilized Enzyme Principles. In Applied Biochemistry and Academic Press, New York.
Trevan, M.D. 1980. Immobilized Enzymes: Introduction and Application in Biotechnology. John Wiley and Sons, New York.
Wang, S.S. and King, C.-K. 1979. The use of coenzymes in biochemical reactors. Adv. Biochem. Bioeng. 12: 119–146.
Chibata, I., Fukui, S. and Wingard, L.B., Jr. (eds.), 1982. Enzyme Engineering, Vol. 6. Plenum Press, New York.
Barman, T.E. 1969. Enzyme Handbook. Springer-Verlag, Berlin.
Lowe, C.R. 1981. Immobilized Coenzymes: Introduction and Application in Biotechnology, p. 13–146. In Topics in Enzyme and Fermentation Technology, Vol. 5. A. Wiseman (ed.). Ellis Horwood, Ltd., Chichester, U.K.
Schmidt, H.L. and Grenner, G. 1976. Coenzyme properties of NAD+ bound to different matrices through the amino group in the 6-position. Eur. J. Biochem. 67: 295–302.
Larsson, P.-O. and Mosbach, K. 1974. The preparation and charac terization of a wafer-soluble coenzymically active dextran-NAD+ FEES Lett. 46: 119–122.
Wandrey, C., Wichmann, R. and Jandel, A.-S. 1982. Mutli-Enzyme Systems in Membrane Reactors, p. 61–67. In Enzyme Engineering, Vol. 6. I. Chibata, S. Fukui, and L. B. Wingard, Jr. (eds.), Plenum Press, New York.
Wichmann, R., Wandrey, C., Buckmann, A.F., and Kula, M.R. 1981. Continuous enzymatic transformation in an enzyme membrane reactor with simultaneous NAD(H) regeneration. Biotechnol. Bioeng. 23: 2789–2802.
Kula, M.-R., Kroner, K.H., Hustedt, H., and Shutte, H. 1982. Scale-up of protein purification by liquid-liquid extraction, p. 69–74. In Enzyme Engineering, Vol. 6. I. Chibata, S. Fukui, and L. B. Wingard, Jr. (eds.), Plenum Press, New York.
Wong, C.-H. and Whitesides, G.M. 1981. Enzyme-catalyzed organic synthesis: NAD(P)H cofactor regeneration by using glucose-6-phos-phate and the glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides. J. Am. Chem. Soc. 103: 4890–4899.
Godbole, S.S., D'Souza, S.F. and Nadkarni, G.B. 1983. Regeneration of NAD(H) by alcohol dehydrogenase in gel-entrapped yeast cells. Enz. Microb. Technol. 5: 125–128.
Yamazaki, Y., Maeda, H., and Kamibayashi, A. 1982. The long-term production of L-malate by the coimmobilized NAD and dehydrogenases. Biotechnol. Bioeng. 24: 1915–1918.
Campbell, J. and Chang, T.M.S. 1976. The recycling of NAD+ (free and immobilized) within semipermeable aqueous microcapsules containing a multi-enzyme system. Biochem. Biophys. Res. Commun. 385: 562–569.
Jones, J.B. and Taylor, K.E. 1976. Nicotinamide coenzyme regeneration. The rates of some 1,4-dihydropyridine, pyridinium salt, and flavin mononucleotide hydrogen-transfer reactions. Can. J. Chem. 54: 2974–2980.
Jones, J.B. and Taylor, K.E. 1973. Use of pyridinium and flavin derivatives for recycling of catalytic amounts of NAD+ during preparative-scale horse liver alcohol dehydrogcnase-catalyzed oxida tion of alcohols. JCS Chem. Comm., p. 205.
Aizawa, M., Coughlin, R.W. and Charles, M. 1975. Electrochemical regeneration of nicotinamide adenine dinucleotide. Biochim. Biophys. Acta 385: 362–370.
Aizawa, M., Suzuki, S., and Kubo, M. 1976. Electrolytic regeneration of NADH from NAD+ with a liquid crystal membrane electrode. Biochim. Biophys. Acta 444: 886–892.
Higgins, I.J., Hammond, R.C., Plotkin, E., Hill, H.A.D., Uosaki, K., Eddowes, M.J., and Cass, A.E.G. 1979. Electroenzymology and biofuel cells, p. 181–193. In Hydrocarbons in Biotechnology. D. E. Harrison, I. J. Higgins, and R. Watkinson (eds.), Institute of Petroleum, London, Heyden and Son, Ltd.
Wingard, L.B., Shaw, C.H. and Castner, J.F. 1982. Bioelectro-chemical fuel cells. Enz. Microb. Technol. 4: 137–142.
Jones, J.B. and Beck, J.F. 1976. Asymmetric syntheses and resolutions using enzymes. Tech. Chem. 10: 107–401.
Jones, J.B. 1980. Enzymes in synthetic organic chemistry, p. 54–81. In Enzymatic and Non-Enzymatic Catalysis. P. Dunhill, A. Wiseman, and N. Blakebrough (eds.), Ellis Horwood, Ltd., Chichester, U.K.
Whitesides, G.M. and Wong, C.H. 1983. Enzymes as catalysts in organic synthesis. Aldrichimica Acta 16: 27–34.
Boyer, P.D. (ed.), 1970. The Enzymes, 3rd. Edition. Academic Press, New York.
Walsh, C. 1979. Enzymatic Reaction Mechanisms. W. H. Freeman and Co., San Francisco.
Boone, J.R. and Ashby, E.C. 1979. Reduction of cyclic and bicyclic ketones by complex metal hydrides, p. 53–95. In Topics in Stereo chemistry, Vol. 11. N. L. Allinger and E. L. Eliel (eds.), John Wiley and Sons, New York.
Wiseman, A. 1981. Alcohol dehydrogenases: immobilisation and applications in analysis and synthesis, p. 337–354. In Topics in Enzyme and Fermentation Biotechnology, Vol. 5. A. Wiseman (ed.), Ellis Horwood, Ltd., Chichester, U.K.
Jones, J.B. 1982. Horse-liver alcohol dehydrogenase: an illustrative example of the potential of enzymes in organic synthesis, p. 107–116. In Enzyme Engineering, Vol. 6. I. Chibata, S. Fukui, and L. B. Wingard, Jr. (eds.), Plenum Press, New York.
Prelog, V. 1964. Specification of the stereospecificity of some oxido-reductases by diamond lattice sections. Pure Appl. Chem. 9: 119–130.
Irwin, A.J. and Jones, J.B. 1977. Regiospecific and enantioselective horse liver alcohol dehydrogenase catalyzed oxidations of some hydroxycyclopentanes. J. Am. Chem. Soc. 99: 1625–1630.
Davies, J. and Jones, J.B. 1979. Enzymes in organic synthesis. 16. Heterocyclic ketones as substrates of horse liver alcohol dehydrogenase. Stereospecific reductions of 2-substituted tetrahydrothiopyran-4-ones. J. Am. Chem. Soc. 101: 5405–5410.
Hou, C.T., Patel, R., Barnabe, N. and Marczak, I. 1981. Stereospecificity and other properties of a novel secondary-alcohol-specific alcohol dehydrogenase. Eur. J. Biochem. 119: 359–364.
Barret, C.H., Dodgson, K.S. and White, G.F. 1981. Specificity and other properties of an alcohol dehydrogenase from Comamonas terrigens, an enzyme exhibiting preference for L-stereoisomers of secondary alcohols. Biochim. Biophys. Acta 661: 74–86.
May, S.W., Steltenkamp, M.S., Borah, K.R., Katopodis, A.G. and Thowsen, J.R. 1979. Enzymatic production of saturated ketones from allylic alcohols. JCS Chem. Comm., p. 845–846.
Lamed, R.J. and Zeikus, J.G. 1981. Novel NADP-linked-aldehyde/ketone oxidoreductase in thermophilic ethanologenic bacteria. Bio-chem. J. 195: 183–190.
Bryant, F. and Ljungdahl, L.G. 1981. Characterization of an alcohol dehydrogenase from Thermoanaerobacter ethanolicus active with ethanol and secondary alcohols. Biochem. Biophys. Res. Comm. 100: 793–799.
Klibanov, A.M., Alberti, B.N. and Zale, S.E. 1982. Enzymatic synthesis of formic acid from H2 and CO2 and production of hydrogen from formic acid. Biotechnol. Bioeng. 24: 25–36.
Danielsson, B., Winqvist, F., Malpote, J.Y. and Mosbach, K. 1982. Regeneration of NADH with immobilized systems of alanine dehydrogenase and hydrogen dehydrogenase. Biotechnol. Lett. 4: 673–678.
Schneider, K. and Schegel, H.G. 1976. Purification and properties of soluble hydrogenase from Alcaligenes eutrophus H16. Biochim. Biophys. Acta 452: 66–80.
Klibanov, A.M. and Puglisi, A.V. 1980. The regeneration of coenzymes using immobilized hydrogenase. Biotechnol. Lett. 2: 445–450.
See reference 9, p. 168.
Brodelius, P. 1978. Industrial applications of immobilized biocatalysts. Adv. Biochem. Bioeng. 10: 75–129.
Chibata, I. 1979. Immobilized microbial cells with polyacrylamide gel and carrageenan and their industrial applications, p. 187–202. In Immobilized Microbial Cells, Vol. 106. K. Venkatsubramanian (ed.), ACS Symposium.
May, S.W. 1979. Enzymatic epoxidation reactions. Enz. Microb. Technol. 1: 15–22.
National Science Foundation. 1974. Workshop on fundamental research in homogeneous catalysis as related to U.S. energy problems, Washington, D.C.
Wiseman, A. and King, D.J. 1982. Microbial oxygenases and their potential application, p. 151–206. In Topics in Enzyme and Fermentation Biotechnology, Vol. 6. A. Wiseman (ed.)
Cain, R.B. 1979. Transformations of organic hydrocarbons, p. 99–132. In Hydrocarbons in Biotechnology, D. E. Harrison, I. J. Higgins, and R. Watkinson (eds.), Institute of Petroleum, London, Heyden and Son, Ltd.
Dalton, H. 1980. Oxidations of hydrocarbons by methane monooxygenases from a variety of microbes. Adv. Appl. Microbiol. 26: 71–87.
Dalton, H. 1979. Transformations by methane monooxygenase, p. 85–97. In Hydrocarbons in Biotechnology, D. E. Harrison, I. J. Higgins, and R. Watkinson (eds.), Institute of Petroleum, London, Heyden and Son, Ltd.
Higgins, I.J., Best, D.J. and Hammond, R.C. 1980. New findings in methane-utilizing bacteria highlight their importance in the biosphere and their commercial potential. Nature 286: 561–564.
Colby, J., Stirling, D.I., and Dalton, H. 1977. The soluble methane monooxygenase of Methylococcus capsulatus (Bath). Biochem. J. 165: 395–402.
Hou, C.-T., Patel, R.N., and Laskin, A.I. 1980. Epoxidation and ketone formation by Cl-utilizing microbes. Adv. App. Microbiol. 26: 41–69.
Patel, R.N., Hou, C.-T., Laskin, A.I., Felix, A. and Derelanko, P. 1980. Microbial oxidation of gaseous hydrocarbons: production of secondary alcohols from corresponding n-alkanes by methane-utilizing bacteria. Appl. Environ. Microbiol. April: 720–726.
Patel, R.N., Hou, C.-T., Laskin, A.I., Felix, A. and Derelanko, P. 1980. Microbial oxidation of gaseous hydrocarbons: production of secondary alcohols from corresponding n-alkanes by methane-utilizing bacteria. Appl. Environ. Microbiol. April: 727–733.
Peterson, J.A., Basu, D. and Coon, M.J. 1966. Enzymatic ω-oxidation. I. Electron carriers in fatty acid and hydrocarbon hydroxylation. J. Biol. Chem. 241: 5162–5164.
May, S.W. and Abbott, B.J. 1972. Enzymatic epoxidation. I. Alkene epoxidation by the ω-hydroxylase system of Pseudomonas oleovorans. Biochem. Biophys. Res. Comm. 48: 1230–1234.
May, S.W. and Abbott, B.J. 1973. Enzymatic epoxidation: comparison between the epoxidation and hydroxylation system of Pseudomonas oleovorans. J. Biol. Chem. 248: 1725–1730.
May, S.W. and Schwartz, R.D. 1974. Stereoselective epoxidation of octadiene catalyzed by an enzyme system of Pseudomonas oleovorans. J. Am. Chem. Soc. 96: 4031.
May, S.W., Steltenkamp, M.S., Schwartz, R.D. and McCoy, C.J. 1976. Stereoselective formation of diepoxides by an enzyme system of Pseudomonas oleovorans. J. Am. Chem. Soc. 98: 7856–7858.
May, S.W., Gordon, S.L. and Steltenkamp, M.S. 1977. Enzymatic epoxidation of trans, trans-l, 8-dideutero-l, 7-octadiene. Analysis using partially relaxed proton fourier transform NMR. J. Am. Chem. Soc. 99: 2017–2024.
See, J.D., Morrison and Mosher, H.S., “Asymmetric Organic Reactions”, Prentice Hall, Englewood Cliffs, NJ, 1971, p. 258–262 and references cited therein, and also G. Berti, Top. Stereochem. 7: 93 (1973). It has long been recognized that the directive effect of allylic alcohols gives rise to varying degrees of stereoselectivity in epoxidation of these compounds by various chemical agents. However, even with the use of chiral epoxidizirig agents, only very low optical yields (ca. 5%) of optically active epoxides are obtained from simple prochiral olelins (such as octadiene).
May, S.W., Wimalasena, K. and Katopodis, A.G. Unpublished results.
deBont, J.A.M., van Ginkel, C.G., Tramper, J., and Luyben, K.Ch.A.M. 1983. Ethylene oxide production by immobilized myco-bacterium pyl in a gas-solid bioreactor. Enz. Microb. Technol. 5: 55–59.
Hou, C.T., Patel, R.N. and Laskin, A.I. 1982. Microbiological epoxidation process. U.S. patent 4,347,319.
Hou, C.T. 1982. Production of epoxides such as propylene oxide using packed catalytic bed containing moist resting cells exhibiting oxygenase activity. U.S. Patent 4,348,476.
deSmet, M.J. 1983. A biotechnological approach to the synthesis of epoxides. Biotechnol. Bioeng. 25: 1161–1162.
Larsson, P.-O., Ohlson, S. and Mosbach, K. 1979. Transformation of steroids by immobilized living microorganisms. Appl. Biochem. Bioeng. 2: 291–301.
Kolot, F.B. 1982. Microbial catalysts for steroid transformations. Part 1. Process Biochem. Nov./Dec.: 12–18.
Koshcheyenko, K.A., Turkina, M.V. and Skryabin, G.K. 1983. Immobilization of living microbial cells and their application for steroid transformations. Enz. Microb. Technol. 5: 14–21.
Demain, A.L. 1981. Industrial microbiology. Science 214: 987–995.
Peterson, D.H. and Murray, H.C. 1952. Microbiological oxygen-ation of steroids at carbon 11. J. Am. Chem. Soc. 74: 1871–1872.
Aharnowitz, Y. and Cohen, G. 1981. The microbiological production of pharmaceuticals. Sci. Am. 245: 141–152.
May, S.W. and Phillips, R.S. 1980. Asymmetric sulfoxidation by dopamine-β-hydroxylase, an oxygenase heretofore considered spe cific for methylene hydroxylation. J. Am. Chem. Soc. 102: 5981–5983.
May, S.W., Phillips, R.S., Mueller, P.W. and Herman, H.H. 1981. Dopamine-β-hydroxylase: comparison of enzymatic ketonization of the product enantiomer, S-octopamine. J. Biol. Chem. 256: 2258–2261.
May, S.W., Phillips, R.S., Herman, H.H. and Mueller, P.M. 1982. Bioactivation of Catha edulis alkaloids: enzymatic ketonization of norpseudoephedrine. Biochem. Biophys. Res. Comm. 104: 38–44.
May, S.S., Phillips, R.S., Mueller, P.M. and Herman, H.H. 1981. Dopamine-β-hydroxylase: comparative specificities and mechanisms of the oxygenation reactions. J. Biol. Chem. 256: 8470–8475.
May, S.W., Mueller, P.W., Padgette, S.R., Herman, H.H. and Phillips, R.S. 1983. Dopamine-β-hydroxylase: suicide inhibition by the novel olefinic substrate, l-phenyl-l-aminomethyletherie. Bio chem. Biophys. Res. Comm. 110: 161–168.
May, S.W. and Roberts, S.F. Unpublished results.
Richter, G. 1983. Glucose oxidase. In Industrial Enzymology. T. Godfrey and J. Reichelt (eds.), Nature Press, New York.
Szwajcer, E., Brodelius, P. and Mosbach, K. 1982. Production of α-keto acids: 2. Immobilized cells of Provedencia sp. PCM 1298 containing L-amino acid oxidase. Enz. Microb. Technol. 4: 409–.
Alberti, B.N. and Klibanov, A.M. 1982. Preparative production of hydroquinone from benzoquinone catalyzed by immobilized D-glucose oxidase. Enz. Microb. Technol. 4: 47–49.
Morrison, M. and Schonbaum, G.R. 1976. Peroxidase-catalyzed reactions. Ann. Rev. Biochem. 45: 935–988.
Manthey, J.A. and Hager, L.P. 1982. Purification and properties of bromoperoxidase from Penicittus capitatus. J. Biol. Chem. 256: 11232–11238.
Geigert, J., Neidleman, S.L., and Dalietos, D.J. 1983. Novel halo-peroxidase substrates. J. Biol. Chem. 258: 2273–2277.
Neidleman, S.L., Amon, W.F. and Geigert, J. 1981. Method of producing epoxides and glycols from alkenes. U.S. Patent 4,247,641.
Eveleigh, D.E. 1981. The microbial production of industrial chemicals. Sci. Am. 245: 155–178.
See reference 90, p. 156.
McElvany, K.D., Knoght, L.C., Welch, M.J., Siuda, J.F., Theiler, R.F. and Hager, L.P. 1979. Use of bromoperoxidase, an algal enzyme, in the preparation of radiobrominated proteins. In Marine Algae in Pharmaceutical Science, H. A. Hoppe, T. Levring, and Y. Tanka (eds.), Walter de Gruyter, Berlin.
Klibanov, A.M., Tu, T.-M. and Scott, K.P. 1983. Peroxidase-catalyzed removal of phenols from coal-conversion waste waters. Science 221: 259–260.
Gloger, M., Nelboeck, M., Doring, D. and Klose, S. 1982. Immobilized enzymes in analysis: applications and economic aspects. Enz. Eng. 6: 377–386.
Pederson, H. and Horvath, C. 1981. Open tubular heterogeneous enzyme reactors in continuous-flow analysis. Appl. Biochem. Bioeng. 3: 1–96.
Wingard, L.B. Jr., Katchalski-Katzir, E. and Goldstein, L. 1981. Analytical Applications of Immobilized Enzymes and Cells. In Applied Biochemistry and Bioengineering, Vol. 3. Academic Press, New York.
Guilbault, G.G. 1982. Analytical uses of immobilized enzymes. Enz. Eng. 6: 395–404.
Suzuki, S. and Karube, I. 1981. Bioelectrochemical sensors based on immobilized enzymes, whole cells, and proteins. Appl. Biochem. Bioeng. 3: 145–174.
Chen, A.K., Liu, C.C. and Schiller, J.G. 1979. Potentiometric method for substrate analysis using immobilized NAD+-dependent oxidoreductase enzymes. Biotechnol. Bioeng. 21: 1905–1915.
Verduyn, C., Van Dijken, J.P. and Scheffers, W.A. 1983. A simple, sensitive, and accurate alcohol electrode. Biolechnol. Bioeng. 25: 1049–1055.
Renneberg, R., Pfiffer, D. and Scheller, F. 1982. Enzyme sequence electrodes based on immobilized glucose oxidase, peroxidase, and catalase. Anal. Chim. Acta. 134: 359–364.
Johnson, J.M., Halsall, H.B. and Heineman, W.R. 1982. Galactose oxidase enzyme electrode with internal solution potential control. Anal. Chem. 54: 1394–1399.
Johnson, J.M., Halsall, H.B. and Heineman, W.R. 1982. Potential-dependent enzymatic activity in an enzyme thin-layer cell. Anal. Chem. 54: 1377–1383.
Enfors, S.-V. 1981. Oxygen-stabilized enzyme electrode for D-glucose analysis in fermentation broths. Enz. Microb. Technol. 3: 29–32.
Tsuchida, T. and Yoda, K. 1982. Immobilization of D-glucose oxidase onto a hydrogen peroxide perrnselective membrane and application for an enzyme electrode. Enz. Microb. Technol. 3: 326–330.
Chotani, G. and Constantinides, A. 1982. On line glucose analyzer for fermentation applications. Biotechnol. Bioeng. 24: 2743–2745.
Kuriyama, S. and Rechitz, G.A. 1981. Plant tissue-based biosclective membrane electrode for glutamate. Anal. Chim. Acta 131: 91–96.
Chen, A.K., Starzmann, J.A. and Lui, C.C. 1982. Potentiometric quantitation of glyccrol using immobilized glycerol dehydrogenase. Biotechnol. Bioeng. 24: 971–975.
Kovach, P.M. and Meyerhoff, M.E. 1982. Development and application of a histidine-selective biomcmbrane electrode. Anal. Chem 54: 217–220.
Wanatabe, E., Ando, K., Karube, I., Matsuoka, H. and Suzuki, S. 1983. Determination of hypoxanthine in fish meat with an enzyme sensor. J. Food Sci. 48: 496–500.
Lui, C.C. and Chen, A.K. 1982. Potentiometric quantitation of biological substrates using gel-immobilized oxidoreductases. Process Biochem. Sept./Oct.: 12–14.
Tran, N.D., Romette, J.L. and Thomas, D. 1983. An enzyme electrode for specific determination of L-lysine: a real-time control sensor. Biotechnol. Bioeng. 25: 329–340.
Clark, L.C. Jr., and Lyons, C. 1962. Electrode systems for continuous monitoring in cardiovascular surgery. Ann. NY Acad. Sci. 102: 29–45.
Slama, J.T., Oruganti, S.R. and Kaiser, E.T. 1981. Semisynthetic enzymes: synthesis of a new' flavopapain with high catalytic efficiency. J. Am. Chem. Soc. 103: 6211–6213.
Schwartz, R.D. 1979. Microbial production of hydroxylated biphenyl compounds. U.S. Patent 4,153,509.
Schwartz, R.D., Williams, A.L. and Hutchinson, D.B. 1980. Microbial production of 4,4′-dihydroxybiphenyl:biphenyl hdyroxylation by fungi. Appl. Env. Microbiol. 39: 702–708.
Schwartz, R.D. and Hutchinson, D.B. 1981. Microbial and enzymatic production of 4,4′-dihydroxybiphenyl via phenol coupling. Enz. Microb. Technol. 3: 361–363.
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May, S., Padgette, S. Oxidoreductase Enzymes in Biotechnology: Current Status and Future Potential. Nat Biotechnol 1, 677–686 (1983). https://doi.org/10.1038/nbt1083-677
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DOI: https://doi.org/10.1038/nbt1083-677
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