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Biochemistry Research International
Volume 2014, Article ID 854687, 16 pages
http://dx.doi.org/10.1155/2014/854687
Review Article

Microbial Tyrosinases: Promising Enzymes for Pharmaceutical, Food Bioprocessing, and Environmental Industry

1Molecular Biotechnology Laboratory, Centre for Scientific Research & Development, People’s University, Bhanpur, Bhopal 462010, India
2Department of Biotechnology, Saifia College of Science, Bhopal 462001, India

Received 3 February 2014; Accepted 31 March 2014; Published 6 May 2014

Academic Editor: Joel H. Weiner

Copyright © 2014 Kamal Uddin Zaidi et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. D. A. Robb, “Tyrosinase,” in Copper Proteins and Copper Enzymes, R. Lontie, Ed., pp. 207–241, CRC Press, Boca Raton, Fla, USA, 1984. View at Google Scholar
  2. J. R. Whitaker, “Polyphenol oxidase,” in Food Enzymes: Structure and Mechanism, D. W. S. Wong, Ed., pp. 271–307, Chapman and Hall, New York, NY, USA, 1995. View at Google Scholar
  3. M. Rolff, J. Schottenheim, H. Decker, and F. Tuczek, “Copper-O2 reactivity of tyrosinase models towards external monophenolic substrates: molecular mechanism and comparison with the enzyme,” Chemical Society Reviews, vol. 40, no. 7, pp. 4077–4098, 2011. View at Publisher · View at Google Scholar · View at Scopus
  4. V. P. S. dos Santos, L. M. C. Silvaa, A. M. Salgado, and K. S. Pereira, “Application of Agaricus bisporusextract for benzoate sodium detection based on tyrosinase inhibition for biosensor development,” Chemical Engineering Transactions, vol. 32, pp. 66–70, 2013. View at Google Scholar
  5. A. Gradilone, E. Cigna, A. M. Agliano, and L. Frati, “Tyrosinase expression as a molecular marker for investigating the presence of circulating tumor cells in melanoma patients,” Current Cancer Drug Targets, vol. 10, no. 5, pp. 529–538, 2010. View at Publisher · View at Google Scholar · View at Scopus
  6. S. Jawaid, T. H. Khan, H. M. I. Osborn, and N. A. O. Williams, “Tyrosinase activated melanoma prodrugs,” Anti-Cancer Agents in Medicinal Chemistry, vol. 9, no. 7, pp. 717–727, 2009. View at Publisher · View at Google Scholar · View at Scopus
  7. E. Monogioudi, G. Faccio, M. Lille, K. Poutanen, J. Buchert, and M.-L. Mattinen, “Effect of enzymatic cross-linking of β-casein on proteolysis by pepsin,” Food Hydrocolloids, vol. 25, no. 1, pp. 71–81, 2011. View at Publisher · View at Google Scholar · View at Scopus
  8. H. Claus and Z. Filip, “Behaviour of phenoloxidases in the presence of clays and other soil-related adsorbents,” Applied Microbiology and Biotechnology, vol. 28, no. 4-5, pp. 506–511, 1988. View at Publisher · View at Google Scholar · View at Scopus
  9. Y.-S. Wang, S.-P. Tian, and Y. Xu, “Effects of high oxygen concentration on pro- and anti-oxidant enzymes in peach fruits during postharvest periods,” Food Chemistry, vol. 91, no. 1, pp. 99–104, 2005. View at Publisher · View at Google Scholar · View at Scopus
  10. S.-Y. Seo, V. K. Sharma, and N. Sharma, “Mushroom tyrosinase: recent prospects,” Journal of Agricultural and Food Chemistry, vol. 51, no. 10, pp. 2837–2853, 2003. View at Publisher · View at Google Scholar · View at Scopus
  11. T.-S. Chang, “An updated review of tyrosinase inhibitors,” International Journal of Molecular Sciences, vol. 10, no. 6, pp. 2440–2475, 2009. View at Publisher · View at Google Scholar · View at Scopus
  12. S. Molloy, J. Nikodinovic-Runic, L. B. Martin et al., “Engineering of a bacterial tyrosinase for improved catalytic efficiency towards D-tyrosine using random and site directed mutagenesis approaches,” Biotechnology and Bioengineering, vol. 110, no. 7, pp. 1849–1857, 2013. View at Publisher · View at Google Scholar
  13. C. W. G. van Gelder, W. H. Flurkey, and H. J. Wichers, “Sequence and structural features of plant and fungal tyrosinases,” Phytochemistry, vol. 45, no. 7, pp. 1309–1323, 1997. View at Publisher · View at Google Scholar · View at Scopus
  14. K. G. Strothkamp, R. L. Jolley, and H. S. Mason, “Quaternary structure of mushroom tyrosinase,” Biochemical and Biophysical Research Communications, vol. 70, no. 2, pp. 519–524, 1976. View at Google Scholar · View at Scopus
  15. K. Lerch, “Copper monooxygenases: tyrosinase and dopamine B-monooxygenase,” in Metal Ions in Biological Systems, H. Sigel, Ed., pp. 143–186, Marcel Dekker, New York, NY, USA, 1983. View at Google Scholar
  16. K. Lerch, “Neurospora tyrosinase: structural, spectroscopic and catalytic properties,” Molecular and Cellular Biochemistry, vol. 52, no. 2, pp. 125–138, 1983. View at Publisher · View at Google Scholar · View at Scopus
  17. L. A. Mueller, U. Hinz, and J.-P. Zrÿd, “Characterization of a tyrosinase from Amanita muscaria involved in betalain biosynthesis,” Phytochemistry, vol. 42, no. 6, pp. 1511–1515, 1996. View at Publisher · View at Google Scholar · View at Scopus
  18. K. Kanda, T. Sato, S. Ishii, H. Enei, and S.-I. Ejiri, “Purification and properties of tyrosinase isozymes from the gill of Lentinus edodes fruiting body,” Bioscience, Biotechnology and Biochemistry, vol. 60, no. 8, pp. 1273–1278, 1996. View at Google Scholar · View at Scopus
  19. M. Nakamura, T. Nakajima, Y. Ohba, S. Yamauchi, B. R. Lee, and E. Ichishima, “Identification of copper ligands in Aspergillus oryzae tyrosinase by site-directed mutagenesis,” Biochemical Journal, vol. 350, no. 2, pp. 537–545, 2000. View at Publisher · View at Google Scholar · View at Scopus
  20. S. Halaouli, M. Asther, K. Kruus et al., “Characterization of a new tyrosinase from Pycnoporus species with high potential for food technological applications,” Journal of Applied Microbiology, vol. 98, no. 2, pp. 332–343, 2005. View at Publisher · View at Google Scholar · View at Scopus
  21. R. O. de Faria, V. R. Moure, W. Balmant, M. A. L. D. A. Amazonas, N. Krieger, and D. A. Mitchell, “The tyrosinase produced by Lentinula boryana (Berk. & Mont.) pegler suffers substrate inhibition by l-DOPA,” Food Technology and Biotechnology, vol. 45, no. 3, pp. 334–340, 2007. View at Google Scholar · View at Scopus
  22. G. Della-Cioppa, S. J. Garger, R. B. Holtz, M. J. Mcculloch, and G. G. Sverlow, “Method for making stable extracellular tyrosinase and synthesis of polyphenolic polymers therefrom,” US Patent 5801047, 1998.
  23. G. Della-Cioppa, S. J. Garger, G. G. Sverlow, T. H. Turpen, L. K. Grill, and M. R. Chedekal, “Melanin production by Streptomyces,” US Patent 5814495, 1998.
  24. Z. Liu, Y. Liu, H. Yang, Y. Yang, G. Shen, and R. Yu, “A phenol biosensor based on immobilizing tyrosinase to modified core-shell magnetic nanoparticles supported at a carbon paste electrode,” Analytica Chimica Acta, vol. 533, no. 1, pp. 3–9, 2005. View at Publisher · View at Google Scholar · View at Scopus
  25. H. Claus and H. Decker, “Bacterial tyrosinases,” Systematic and Applied Microbiology, vol. 29, no. 1, pp. 3–14, 2006. View at Publisher · View at Google Scholar · View at Scopus
  26. A. M. McMahon, E. M. Doyle, S. Brooks, and K. E. O'Connor, “Biochemical characterisation of the coexisting tyrosinase and laccase in the soil bacterium Pseudomonas putida F6,” Enzyme and Microbial Technology, vol. 40, no. 5, pp. 1435–1441, 2007. View at Publisher · View at Google Scholar · View at Scopus
  27. Y. Matoba, T. Kumagai, A. Yamamoto, H. Yoshitsu, and M. Sugiyama, “Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis,” The Journal of Biological Chemistry, vol. 281, no. 13, pp. 8981–8990, 2006. View at Publisher · View at Google Scholar · View at Scopus
  28. A. Janovitz-Klapp, F. Richard, and J. Nicolas, “Polyphenoloxidase from apple, partial purification and some properties,” Phytochemistry, vol. 28, no. 11, pp. 2903–2907, 1989. View at Google Scholar · View at Scopus
  29. J. Raymond, N. Rakariyatham, and J. L. Azanza, “Purification and some properties of polyphenoloxidase from sunflower seeds,” Phytochemistry, vol. 34, no. 4, pp. 927–931, 1993. View at Publisher · View at Google Scholar · View at Scopus
  30. J.-L. Lee, K.-H. Kong, and S.-H. Cho, “Purification and characterization of tyrosinase from Solanum melongena,” Journal of Biochemistry and Molecular Biology, vol. 30, no. 2, pp. 150–156, 1997. View at Google Scholar · View at Scopus
  31. M. Friedman, “Food browning and its prevention: an overview,” Journal of Agricultural and Food Chemistry, vol. 44, no. 3, pp. 631–653, 1996. View at Google Scholar · View at Scopus
  32. I. Kubo and I. Kinst-Hori, “Tyrosinase inhibitors from cumin,” Journal of Agricultural and Food Chemistry, vol. 46, no. 12, pp. 5338–5341, 1998. View at Google Scholar · View at Scopus
  33. N. Rani, B. Joy, and T. E. Abraham, “Cell suspension cultures of Portulaca grandiflora. as potent catalysts for biotransformation of L-tyrosine into L-DOPA, an anti-Parkinson's drug,” Pharmaceutical Biology, vol. 45, no. 1, pp. 48–53, 2007. View at Publisher · View at Google Scholar · View at Scopus
  34. A. M. Mayer, “Polyphenol oxidases in plants and fungi: going places? A review,” Phytochemistry, vol. 67, no. 21, pp. 2318–2331, 2006. View at Publisher · View at Google Scholar · View at Scopus
  35. E. Jaenicke and H. Decker, “Tyrosinases from crustaceans form hexamers,” Biochemical Journal, vol. 371, no. 2, pp. 515–523, 2003. View at Publisher · View at Google Scholar · View at Scopus
  36. R. L. Jolley Jr., D. A. Robb, and H. S. Mason, “The multiple forms of mushroom tyrosinase: association-dissociation phenomena,” The Journal of Biological Chemistry, vol. 244, no. 6, pp. 1593–1599, 1969. View at Google Scholar · View at Scopus
  37. J. Wu, H. Chen, J. Gao, X. Liu, W. Cheng, and X. Ma, “Cloning, characterization and expression of two new polyphenol oxidase cDNAs from Agaricus bisporus,” Biotechnology Letters, vol. 32, no. 10, pp. 1439–1447, 2010. View at Publisher · View at Google Scholar · View at Scopus
  38. K. Nishioka, “Particulate tyrosinase of human malignant melanoma. Solubilization, purification following trypsin treatment, and characterization,” European Journal of Biochemistry, vol. 85, no. 1, pp. 137–146, 1978. View at Google Scholar · View at Scopus
  39. P. F. T. Vaughan, R. Eason, J. Y. Paton, and G. A. Ritchie, “Molecular weight and amino acid composition of purified spinach beet phenolase,” Phytochemistry, vol. 14, no. 11, pp. 2383–2386, 1975. View at Google Scholar · View at Scopus
  40. E. I. Solomon, U. M. Sundaram, and T. E. Machonkin, “Multicopper oxidases and oxygenases,” Chemical Reviews, vol. 96, no. 7, pp. 2563–2605, 1996. View at Google Scholar · View at Scopus
  41. D. E. Wilcox, A. G. Porras, Y. T. Hwang, K. Lerch, M. E. Winkler, and E. I. Solomon, “Substrate analogue binding to the coupled binuclear copper active site in tyrosinase,” Journal of the American Chemical Society, vol. 107, no. 13, pp. 4015–4027, 1985. View at Google Scholar · View at Scopus
  42. Á. Sánchez-Ferrer, J. N. Rodríguez-López, F. García-Cánovas, and F. García-Carmona, “Tyrosinase: a comprehensive review of its mechanism,” Biochimica Biophysica Acta, vol. 1247, no. 1, pp. 1–11, 1995. View at Google Scholar
  43. T. G. Pridham, P. Anderson, C. Foley, L. A. Lindenfelser, C. W. Hesseltine, and R. G. Benedict, “A selection of media for maintenance and taxonomic study of Streptomyces,” Antibiotics Annual, vol. 57, pp. 947–953, 1957. View at Google Scholar
  44. M. Sendovski, M. Kanteev, V. S. Ben-Yosef, N. Adir, and A. Fishman, “First structures of an active bacterial tyrosinase reveal copper plasticity,” Journal of Molecular Biology, vol. 405, no. 1, pp. 227–237, 2011. View at Publisher · View at Google Scholar · View at Scopus
  45. M. Fairhead and L. Thöny-Meyer, “Role of the C-terminal extension in a bacterial tyrosinase,” The FEBS Journal, vol. 277, no. 9, pp. 2083–2095, 2010. View at Publisher · View at Google Scholar · View at Scopus
  46. Y. Kawamura-Konishi, M. Tsuji, S. Hatana et al., “Purification, characterization, and molecular cloning of tyrosinase from Pholiota nameko,” Bioscience, Biotechnology and Biochemistry, vol. 71, no. 7, pp. 1752–1760, 2007. View at Publisher · View at Google Scholar · View at Scopus
  47. Y. Fujita, Y. Uraga, and E. Ichisima, “Molecular cloning and nucleotide sequence of the protyrosinase gene, melO, from Aspergillus orzyae and expression of the gene in yeast cells,” Biochimica et Biophysica Acta, vol. 1261, no. 1, pp. 151–154, 1995. View at Publisher · View at Google Scholar · View at Scopus
  48. J. C. Espín, P. A. García-Ruiz, J. Tudela, and F. García-Cánovas, “Study of stereospecificity in mushroom tyrosinase,” Biochemical Journal, vol. 331, no. 2, pp. 547–551, 1998. View at Google Scholar · View at Scopus
  49. A. Sánchez-Ferrer, J. Villalba, and F. García-Carmona, “Triton X-114 as a tool for purifying spinach polyphenol oxidase,” Phytochemistry, vol. 28, no. 5, pp. 1321–1325, 1989. View at Google Scholar · View at Scopus
  50. Á. Sánchez-Ferrer, R. Bru, and F. García-Carmona, “Partial purification of a thylakoid-bound enzyme using temperature-induced phase partitioning,” Analytical Biochemistry, vol. 184, no. 2, pp. 279–282, 1990. View at Google Scholar · View at Scopus
  51. J. D. Laskin and L. A. Piccinini, “Tyrosinase isozyme heterogeneity in differentiating B16/C3 melanoma,” The Journal of Biological Chemistry, vol. 261, no. 35, pp. 16626–16635, 1986. View at Google Scholar · View at Scopus
  52. J. Cabanes, F. García-Cánovas, J. A. Lozano, and F. García-Carmona, “A kinetic study of the melanization pathway between l-tyrosine and dopachrome,” Biochimica et Biophysica Acta, vol. 923, no. 2, pp. 187–195, 1987. View at Google Scholar · View at Scopus
  53. J. C. Espín, R. Varón, L. G. Fenoll et al., “Kinetic characterization of the substrate specificity and mechanism of mushroom tyrosinase,” European Journal of Biochemistry, vol. 267, no. 5, pp. 1270–1279, 2000. View at Publisher · View at Google Scholar · View at Scopus
  54. V. J. Hearing and M. Jiménez, “Mammalian tyrosinase—the critical regulatory control point in melanocyte pigmentation,” International Journal of Biochemistry, vol. 19, no. 12, pp. 1141–1147, 1987. View at Google Scholar · View at Scopus
  55. X. Wan, B. Chai, Y. Liao et al., “Molecular and biochemical characterization of a distinct tyrosinase involved in melanin production from Aeromonas media,” Applied Microbiology and Biotechnology, vol. 82, no. 2, pp. 261–269, 2009. View at Publisher · View at Google Scholar · View at Scopus
  56. F. Gandía-Herrero, F. García-Carmona, and J. Escribano, “Purification and characterization of a latent polyphenol oxidase from beet root (Beta vulgaris L.),” Journal of Agricultural and Food Chemistry, vol. 52, no. 3, pp. 609–615, 2004. View at Google Scholar · View at Scopus
  57. E. Selinheimo, D. NiEidhin, C. Steffensen et al., “Comparison of the characteristics of fungal and plant tyrosinases,” Journal of Biotechnology, vol. 130, no. 4, pp. 471–480, 2007. View at Publisher · View at Google Scholar · View at Scopus
  58. L. G. Fenoll, M. J. Peñalver, J. N. Rodríguez-López, R. Varón, F. García-Cánovas, and J. Tudela, “Tyrosinase kinetics: discrimination between two models to explain the oxidation mechanism of monophenol and diphenol substrates,” The International Journal of Biochemistry & Cell Biology, vol. 36, no. 2, pp. 235–246, 2004. View at Publisher · View at Google Scholar · View at Scopus
  59. F. García-Molina, M. J. Peñalver, J. N. Rodríguez-López, F. García-Cánovas, and J. Tudela, “Enzymatic method with polyphenol oxidase for the determination of cysteine and N-acetylcysteine,” Journal of Agricultural and Food Chemistry, vol. 53, no. 16, pp. 6183–6189, 2005. View at Publisher · View at Google Scholar · View at Scopus
  60. C. E. Birse and A. J. Clutterbuck, “N-acetyl-6-hydroxytryptophan oxidase, a developmentally controlled phenol oxidase from Aspergillus nidulans,” Journal of General Microbiology, vol. 136, no. 9, pp. 1725–1730, 1990. View at Google Scholar · View at Scopus
  61. V. Shuster and A. Fishman, “Isolation, cloning and characterization of a tyrosinase with improved activity in organic solvents from Bacillus megaterium,” Journal of Molecular Microbiology and Biotechnology, vol. 17, no. 4, pp. 188–200, 2009. View at Publisher · View at Google Scholar · View at Scopus
  62. M. Ito and K. Oda, “An organic solvent resistant tyrosinase from Streptomyces sp. REN-21: purification and characterization,” Bioscience, Biotechnology and Biochemistry, vol. 64, no. 2, pp. 261–267, 2000. View at Google Scholar · View at Scopus
  63. E. Selinheimo, M. Saloheimo, E. Ahola et al., “Production and characterization of a secreted, C-terminally processed tyrosinase from the filamentous fungus Trichoderma reesei,” The FEBS Journal, vol. 273, no. 18, pp. 4322–4335, 2006. View at Publisher · View at Google Scholar · View at Scopus
  64. H. Kamahldin, R. J. Ferdous, K. Ali-Asghar, and S. B. Shahrzad, “Purification of tyrosinase from edible mushroom,” Iranian Journal of Biotechnology, vol. 2, no. 3, pp. 189–194, 2004. View at Google Scholar
  65. S. Koga, M. Nakano, and S. Tero-Kubota, “Generation of superoxide during the enzymatic action of tyrosinase,” Archives of Biochemistry and Biophysics, vol. 292, no. 2, pp. 570–575, 1992. View at Publisher · View at Google Scholar · View at Scopus
  66. J. C. Espín, R. Varón, J. Tudela, and F. García-Cánovas, “Kinetic study of the oxidation of 4-hydroxyanisole catalyzed by tyrosinase,” Biochemistry and Molecular Biology International, vol. 41, no. 6, pp. 1265–1276, 1997. View at Google Scholar · View at Scopus
  67. S. Bouchilloux, P. Mcmahill, and H. S. Mason, “The multiple forms of mushroom tyrosinase. Purification and molecular properties of the enzymes,” The Journal of Biological Chemistry, vol. 238, pp. 1699–1707, 1963. View at Google Scholar · View at Scopus
  68. Y. Fan and W. H. Flurkey, “Purification and characterization of tyrosinase from gill tissue of Portabella mushrooms,” Phytochemistry, vol. 65, no. 6, pp. 671–678, 2004. View at Publisher · View at Google Scholar · View at Scopus
  69. H. J. Wichers, Y. A. M. Gerritsen, and C. G. J. Chapelon, “Tyrosinase isoforms from the fruitbodies of Agaricus bisporus,” Phytochemistry, vol. 43, no. 2, pp. 333–337, 1996. View at Publisher · View at Google Scholar · View at Scopus
  70. V. del Marmol and F. Beermann, “Tyrosinase and related proteins in mammalian pigmentation,” FEBS Letters, vol. 381, no. 3, pp. 165–168, 1996. View at Publisher · View at Google Scholar · View at Scopus
  71. F. Solano, S. Briganti, M. Picardo, and G. Ghanem, “Hypopigmenting agents: an updated review on biological, chemical and clinical aspects,” Pigment Cell Research, vol. 19, no. 6, pp. 550–571, 2006. View at Publisher · View at Google Scholar · View at Scopus
  72. K. Ray, M. Chaki, and M. Sengupta, “Tyrosinase and ocular diseases: some novel thoughts on the molecular basis of oculocutaneous albinism type 1,” Progress in Retinal and Eye Research, vol. 26, no. 4, pp. 323–358, 2007. View at Publisher · View at Google Scholar · View at Scopus
  73. M. Sugumaran, “Comparative biochemistry of eumelanogenesis and the protective roles of phenoloxidase and melanin in insects,” Pigment Cell Research, vol. 15, no. 1, pp. 2–9, 2002. View at Publisher · View at Google Scholar · View at Scopus
  74. A. A. Khan, S. Akhtar, and Q. Husain, “Simultaneous purification and immobilization of mushroom tyrosinase on an immunoaffinity support,” Process Biochemistry, vol. 40, no. 7, pp. 2379–2386, 2005. View at Publisher · View at Google Scholar · View at Scopus
  75. E. Ichishima, H. Maeba, T. Amikura, and H. Sakata, “Multiple forms of protyrosinase from Aspergillus oryzae and their mode of activation at pH 3.0,” Biochimica et Biophysica Acta, vol. 786, no. 1-2, pp. 25–31, 1984. View at Google Scholar · View at Scopus
  76. G. S. Gukasyan, “Purification and some properties of tyrosinase from Aspergillus flavipes 56003,” Biochemistry, vol. 64, no. 4, pp. 417–420, 1999. View at Google Scholar · View at Scopus
  77. M. Fling, N. H. Horowitz, and S. F. Heinemann, “The isolation and properties of crystalline tyrosinase from Neurospora,” The Journal of Biological Chemistry, vol. 238, pp. 2045–2053, 1963. View at Google Scholar · View at Scopus
  78. Y.-J. Kim and H. Uyama, “Tyrosinase inhibitors from natural and synthetic sources: structure, inhibition mechanism and perspective for the future,” Cellular and Molecular Life Sciences, vol. 62, no. 15, pp. 1707–1723, 2005. View at Publisher · View at Google Scholar · View at Scopus
  79. Summers, “A lightening tour of skin brightening option,” South African Pharmaceutical and Cosmetic Review, vol. 33, no. 6, pp. 29–30, 2006. View at Google Scholar
  80. N. Baurin, E. Arnoult, T. Scior, Q. T. Do, and P. Bernard, “Preliminary screening of some tropical plants for anti-tyrosinase activity,” Journal of Ethnopharmacology, vol. 82, no. 2-3, pp. 155–158, 2002. View at Publisher · View at Google Scholar · View at Scopus
  81. H. S. Mason, “The chemistry of melanin: III. Mechanism of the oxidation of trihydroxyphenylalanine by tyrosinase,” The Journal of Biological Chemistry, vol. 172, pp. 83–99, 1948. View at Google Scholar
  82. K.-H. Wang, R.-D. Lin, F.-L. Hsu et al., “Cosmetic applications of selected traditional Chinese herbal medicines,” Journal of Ethnopharmacology, vol. 106, no. 3, pp. 353–359, 2006. View at Publisher · View at Google Scholar · View at Scopus
  83. O. Nerya, J. Vaya, R. Musa, S. Izrael, R. Ben-Arie, and S. Tamir, “Glabrene and isoliquiritigenin as tyrosinase inhibitors from licorice roots,” Journal of Agricultural and Food Chemistry, vol. 51, no. 5, pp. 1201–1207, 2003. View at Publisher · View at Google Scholar · View at Scopus
  84. Ikram-ul-Haq, S. Ali, and M. A. Qadeer, “Biosynthesis of l-DOPA by Aspergillus oryzae,” Bioresource Technology, vol. 85, no. 1, pp. 25–29, 2002. View at Publisher · View at Google Scholar · View at Scopus
  85. V. C. Sanz, M. L. Mena, A. González-Cortés, P. Yáñez-Sedeño, and J. M. Pingarrón, “Development of a tyrosinase biosensor based on gold nanoparticles-modified glassy carbon electrodes: application to the measurement of a bioelectrochemical polyphenols index in wines,” Analytica Chimica Acta, vol. 528, no. 1, pp. 1–8, 2005. View at Publisher · View at Google Scholar · View at Scopus
  86. P. Pialis and B. A. Saville, “Production of l-DOPA from tyrosinase immobilized on nylon 6,6: enzyme stability and scaleup,” Enzyme and Microbial Technology, vol. 22, no. 4, pp. 261–268, 1998. View at Publisher · View at Google Scholar · View at Scopus
  87. S. Ates, E. Cortenlioglu, E. Bayraktar, and U. Mehmetoglu, “Production of l-DOPA using Cu-alginate gel immobilized tyrosinase in a batch and packed bed reactor,” Enzyme and Microbial Technology, vol. 40, no. 4, pp. 683–687, 2007. View at Publisher · View at Google Scholar · View at Scopus
  88. T. Koyanagi, T. Katayama, H. Suzuki, H. Nakazawa, K. Yokozeki, and H. Kumagai, “Effective production of 3,4-dihydroxyphenyl-l (l-DOPA) with Erwinia herbicola cells carrying a mutant transcriptional regulator TyrR,” Journal of Biotechnology, vol. 115, no. 3, pp. 303–306, 2005. View at Publisher · View at Google Scholar · View at Scopus
  89. T. Katayama and H. Kumagai, “l-DOPA, microbial production,” in Encyclopedia of Industrial Biotechnology Bioprocess, Bioseparation, and Cell Technology, pp. 1–4, 2010. View at Publisher · View at Google Scholar
  90. Ikram-ul-Haq and S. Ali, “Mutation of Aspergillus oryzae for improved production of 3, 4-dihydroxy phenyl-l-alanine (l-DOPA) from l-tyrosine,” Brazilian Journal of Microbiology, vol. 37, no. 1, pp. 78–86, 2006. View at Publisher · View at Google Scholar · View at Scopus
  91. S. Ali, J. L. Shultz, and Ikram-ul-Haq, “High performance microbiological transformation of l-tyrosine to l-DOPA by Yarrowia lipolytica NRRL-143,” BMC Biotechnology, vol. 7, article 50, 2007. View at Publisher · View at Google Scholar · View at Scopus
  92. R. Krishnaveni, V. Rathod, M. S. Thakur, and Y. F. Neelgund, “Transformation of l-tyrosine to l-DOPA by a novel fungus, Acremonium rutilum, under submerged fermentation,” Current Microbiology, vol. 58, no. 2, pp. 122–128, 2009. View at Publisher · View at Google Scholar · View at Scopus
  93. S. N. Surwase and J. P. Jadhav, “Bioconversion of l-tyrosine to l-DOPA by a novel bacterium Bacillus sp. JPJ,” Amino Acids, vol. 41, no. 2, pp. 495–506, 2011. View at Publisher · View at Google Scholar · View at Scopus
  94. T. Chen, H. D. Embree, L.-Q. Wu, and G. F. Payne, “In vitro protein-polysaccharide conjugation: tyrosinase-catalyzed conjugation of gelatin and chitosan,” Biopolymers, vol. 64, no. 6, pp. 292–302, 2002. View at Publisher · View at Google Scholar · View at Scopus
  95. M. E. Morrison, M. J. Yagi, and G. Cohen, “In vitro studies of 2,4-dihydroxyphenylalanine, a prodrug targeted against malignant melanoma cells,” Proceedings of the National Academy of Sciences of the United States of America, vol. 82, no. 9, pp. 2960–2964, 1985. View at Google Scholar · View at Scopus
  96. A. M. Jordan, T. H. Khan, H. M. I. Osborn, A. Photiou, and P. A. Riley, “Melanocyte-directed enzyme prodrug therapy (MDEPT): development of a targeted treatment for malignant melanoma,” Bioorganic & Medicinal Chemistry, vol. 7, no. 9, pp. 1775–1780, 1999. View at Publisher · View at Google Scholar · View at Scopus
  97. A. Anghileri, R. Lantto, K. Kruus, C. Arosio, and G. Freddi, “Tyrosinase-catalyzed grafting of sericin peptides onto chitosan and production of protein-polysaccharide bioconjugates,” Journal of Biotechnology, vol. 127, no. 3, pp. 508–519, 2007. View at Publisher · View at Google Scholar · View at Scopus
  98. C. Brasquet, E. Subrenat, and P. le Cloirec, “Removal of phenolic compounds from aqueous solution by activated carbon cloths,” Water Science and Technology, vol. 39, no. 10-11, pp. 201–205, 1999. View at Publisher · View at Google Scholar · View at Scopus
  99. N. Singh and J. Singh, “An enzymatic method for removal of phenol from industrial effluent,” Preparative Biochemistry & Biotechnology, vol. 32, no. 2, pp. 127–133, 2002. View at Publisher · View at Google Scholar · View at Scopus
  100. K. Ikehata and J. A. Nicell, “Color and toxicity removal following tyrosinase-catalyzed oxidation of phenols,” Biotechnology Progress, vol. 16, no. 4, pp. 533–540, 2000. View at Publisher · View at Google Scholar · View at Scopus
  101. S. M. Marino, S. Fogal, M. Bisaglia et al., “Investigation of Streptomyces antibioticus tyrosinase reactivity toward chlorophenols,” Archives of Biochemistry and Biophysics, vol. 505, no. 1, pp. 67–74, 2011. View at Publisher · View at Google Scholar · View at Scopus
  102. J. P. Jadhav, D. C. Kalyani, A. A. Telke, S. S. Phugare, and S. P. Govindwar, “Evaluation of the efficacy of a bacterial consortium for the removal of color, reduction of heavy metals, and toxicity from textile dye effluent,” Bioresource Technology, vol. 101, no. 1, pp. 165–173, 2010. View at Publisher · View at Google Scholar · View at Scopus
  103. R. G. Saratale, G. D. Saratale, J. S. Chang, and S. P. Govindwar, “Bacterial decolorization and degradation of azo dyes: a review,” Journal of the Taiwan Institute of Chemical Engineers, vol. 42, no. 1, pp. 138–157, 2011. View at Publisher · View at Google Scholar · View at Scopus
  104. J. V. Bevilaqua, M. C. Cammarota, D. M. G. Freire, and G. L. Santanna Jr., “Phenol removal through combined biological and enzymatic treatments,” Brazilian Journal of Chemical Engineering, vol. 19, no. 2, pp. 151–158, 2002. View at Google Scholar · View at Scopus
  105. H. Xue and Z. Shen, “A highly stable biosensor for phenols prepared by immobilizing polyphenol oxidase into polyaniline-polyacrylonitrile composite matrix,” Talanta, vol. 57, no. 2, pp. 289–295, 2002. View at Publisher · View at Google Scholar · View at Scopus
  106. J. Yu, S. Liu, and H. Ju, “Mediator-free phenol sensor based on titania sol-gel encapsulation matrix for immobilization of tyrosinase by a vapor deposition method,” Biosensors and Bioelectronics, vol. 19, no. 5, pp. 509–514, 2003. View at Publisher · View at Google Scholar · View at Scopus
  107. K. Yamada, Y. Akiba, T. Shibuya, A. Kashiwada, K. Matsuda, and M. Hirata, “Water purification through bioconversion of phenol compounds by tyrosinase and chemical adsorption by chitosan beads,” Biotechnology Progress, vol. 21, no. 3, pp. 823–829, 2005. View at Publisher · View at Google Scholar · View at Scopus
  108. G. A. Rivas and V. M. Solis, “Indirect electrochemical determination of l-tyrosine using mushroom tyrosinase in solution,” Analytical Chemistry, vol. 63, no. 23, pp. 2762–2765, 1991. View at Google Scholar · View at Scopus
  109. A. I. Yaropolov, A. N. Kharybin, J. Emnéus, G. Marko-Varga, and L. Gorton, “Flow-injection analysis of phenols at a graphite electrode modified with co-immobilised laccase and tyrosinase,” Analytica Chimica Acta, vol. 308, no. 1–3, pp. 137–144, 1995. View at Publisher · View at Google Scholar · View at Scopus
  110. C. R. Tillyer and P. T. Gobin, “The development of a catechol enzyme electrode and its possible use for the diagnosis and monitoring of neural crest tumours,” Biosensors and Bioelectronics, vol. 6, no. 7, pp. 569–573, 1991. View at Publisher · View at Google Scholar · View at Scopus
  111. G. Wang, J.-J. Xu, L.-H. Ye, J.-J. Zhu, and H.-Y. Chen, “Highly sensitive sensors based on the immobilization of tyrosinase in chitosan,” Bioelectrochemistry, vol. 57, no. 1, pp. 33–38, 2002. View at Publisher · View at Google Scholar · View at Scopus
  112. J. Wang, L. Fang, and D. Lopez, “Amperometric biosensor for phenols based on a tyrosinase-graphite-epoxy biocomposite,” Analyst, vol. 119, no. 3, pp. 455–458, 1994. View at Google Scholar · View at Scopus
  113. J. Wang, F. Lu, and D. Lopez, “Tyrosinase-based ruthenium dispersed carbon paste biosensor for phenols,” Biosensors and Bioelectronics, vol. 9, no. 1, pp. 9–15, 1994. View at Publisher · View at Google Scholar · View at Scopus
  114. P. Önnerfjord, J. Emnéus, G. Marko-Varga, and L. Gorton, “Tyrosinase graphite-epoxy based composite electrodes for detection of phenols,” Biosensors and Bioelectronics, vol. 10, no. 6-7, pp. 607–619, 1995. View at Publisher · View at Google Scholar · View at Scopus
  115. C. Védrine, S. Fabiano, and C. Tran-Minh, “Amperometric tyrosinase based biosensor using an electrogenerated polythiophene film as an entrapment support,” Talanta, vol. 59, no. 3, pp. 535–544, 2003. View at Publisher · View at Google Scholar · View at Scopus
  116. R. Rajesh, W. Takashima, and K. Kaneto, “Amperometric tyrosinase based biosensor using an electropolymerized PTS-doped polypyrrole film as an entrapment support,” Reactive & Functional Polymers, vol. 59, no. 2, pp. 163–169, 2004. View at Publisher · View at Google Scholar · View at Scopus
  117. S. Campuzano, B. Serra, M. Pedrero, F. J. M. de Villena, and J. M. Pingarrón, “Amperometric flow-injection determination of phenolic compounds at self-assembled monolayer-based tyrosinase biosensors,” Analytica Chimica Acta, vol. 494, no. 1-2, pp. 187–197, 2003. View at Publisher · View at Google Scholar · View at Scopus
  118. T. Tatsuma and T. Sato, “Self-wiring from tyrosinase to an electrode with redox polymers,” Journal of Electroanalytical Chemistry, vol. 572, no. 1, pp. 15–19, 2004. View at Publisher · View at Google Scholar · View at Scopus
  119. Z. Liu, B. Liu, J. Kong, and J. Deng, “Probing trace phenols based on mediator-free alumina sol-gel-derived tyrosinase biosensor,” Analytical Chemistry, vol. 72, no. 19, pp. 4707–4712, 2000. View at Publisher · View at Google Scholar · View at Scopus
  120. Y.-F. Li, Z.-M. Liu, Y.-L. Liu, Y.-H. Yang, G.-L. Shen, and R.-Q. Yu, “A mediator-free phenol biosensor based on immobilizing tyrosinase to ZnO nanoparticles,” Analytical Biochemistry, vol. 349, no. 1, pp. 33–40, 2006. View at Publisher · View at Google Scholar · View at Scopus
  121. S. Tembe, M. Karve, S. Inamdar, S. Haram, J. Melo, and S. F. D'Souza, “Development of electrochemical biosensor based on tyrosinase immobilized in composite biopolymeric film,” Analytical Biochemistry, vol. 349, no. 1, pp. 72–77, 2006. View at Publisher · View at Google Scholar · View at Scopus
  122. G. B. Seetharam and B. A. Saville, “Degradation of phenol using tyrosinase immobilized on siliceous supports,” Water Research, vol. 37, no. 2, pp. 436–440, 2003. View at Publisher · View at Google Scholar · View at Scopus
  123. S. R. Ahmed, A. T. Lutes, and T. A. Barbari, “Specific capture of target proteins by oriented antibodies bound to tyrosinase-immobilized Protein A on a polyallylamine affinity membrane surface,” Journal of Membrane Science, vol. 282, no. 1-2, pp. 311–321, 2006. View at Publisher · View at Google Scholar · View at Scopus
  124. J. L. H. C. Busch, K. Hrncirik, E. Bulukin, C. Boucon, and M. Mascini, “Biosensor measurements of polar phenolics for the assessment of the bitterness and pungency of virgin olive oil,” Journal of Agricultural and Food Chemistry, vol. 54, no. 12, pp. 4371–4377, 2006. View at Publisher · View at Google Scholar · View at Scopus
  125. K. Streffer, E. Vijgenboom, A. W. J. W. Tepper et al., “Determination of phenolic compounds using recombinant tyrosinase from Streptomyces antibioticus,” Analytica Chimica Acta, vol. 427, no. 2, pp. 201–210, 2001. View at Publisher · View at Google Scholar · View at Scopus
  126. F. Ortega, E. Domínguez, E. Burestedt, J. Emnéus, L. Gorton, and G. Marko-Varga, “Phenol oxidase-based biosensors as selective detection units in column liquid chromatography for the determination of phenolic compounds,” Journal of Chromatography A, vol. 675, no. 1-2, pp. 65–78, 1994. View at Publisher · View at Google Scholar · View at Scopus
  127. J.-L. Marty, K. Sode, and I. Karube, “Biosensor for detection of organophosphate and carbamate insecticides,” Electroanalysis, vol. 4, no. 2, pp. 249–252, 1992. View at Publisher · View at Google Scholar
  128. T. Shekhovtsova and S. Chernetskaya, “Determination of mercury at the picogram per milliliter level using immobilized horseradish peroxidase,” Analytical Letters, vol. 27, no. 15, pp. 2883–2898, 1994. View at Publisher · View at Google Scholar
  129. C. M. Aberg, T. Chen, A. Olumide, S. R. Raghavan, and G. F. Payne, “Enzymatic grafting of peptides from casein hydrolysate to chitosan. Potential for value-added byproducts from food-processing wastes,” Journal of Agricultural and Food Chemistry, vol. 52, no. 4, pp. 788–793, 2004. View at Publisher · View at Google Scholar · View at Scopus
  130. J. Huang, C. Liu, H. Xiao, J. Wang, D. Jiang, and E. Gu, “Zinc tetraaminophthalocyanine-Fe3O4 nanoparticle composite for laccase immobilization,” International Journal of Nanomedicine, vol. 2, no. 4, pp. 775–784, 2007. View at Google Scholar · View at Scopus
  131. L. Tang, G. Zeng, J. Liu et al., “Catechol determination in compost bioremediation using a laccase sensor and artificial neural networks,” Analytical & Bioanalytical Chemistry, vol. 391, no. 2, pp. 679–685, 2008. View at Publisher · View at Google Scholar · View at Scopus
  132. S. Wang, Y. Tan, D. Zhao, and G. Liu, “Amperometric tyrosinase biosensor based on Fe3O4 nanoparticles-chitosan nanocomposite,” Biosensors and Bioelectronics, vol. 23, no. 12, pp. 1781–1787, 2008. View at Publisher · View at Google Scholar · View at Scopus
  133. L. M. Rossi, A. D. Quach, and Z. Rosenzweig, “Glucose oxidase-magnetite nanoparticle bioconjugate for glucose sensing,” Analytical & Bioanalytical Chemistry, vol. 380, no. 4, pp. 606–613, 2004. View at Publisher · View at Google Scholar · View at Scopus
  134. J. Qiu, H. Peng, and R. Liang, “Ferrocene-modified Fe3O4@SiO2 magnetic nanoparticles as building blocks for construction of reagentless enzyme-based biosensors,” Electrochemistry Communications, vol. 9, no. 11, pp. 2734–2738, 2007. View at Publisher · View at Google Scholar · View at Scopus
  135. S. Motamed, F. Ghaemmaghami, and I. Alemzadeh, “Turnip (Brassica rapa) peroxidase: purification and characterization,” Industrial & Engineering Chemistry Research, vol. 48, no. 23, pp. 10614–10618, 2009. View at Publisher · View at Google Scholar · View at Scopus
  136. S. E. Stanca, I. C. Popescuo, and L. Oniciu, “Biosensors for phenol derivatives using biochemical signal amplification,” Talanta, vol. 61, no. 4, pp. 501–507, 2003. View at Publisher · View at Google Scholar · View at Scopus
  137. M. Kawakami, H. Koya, K. Amada, and M. Shimojo, “Amperometric 2,4-dichlorophenoxyacetate biosensor system based on a microbial reactor and a tyrosinase-modified electrode,” Analytical Letters, vol. 40, no. 5, pp. 921–932, 2007. View at Publisher · View at Google Scholar · View at Scopus
  138. R. Rastall, Novel Enzyme Technology for Food Applications, Woodhead Publishing, Cambridge, UK, 2007.
  139. J. Buchert, E. Selinheimo, K. Kruus, M. L. Mattinen, R. Lantto, and K. Autio, “Cross-linking enzymes in food processing,” in Novel Enzyme Technology for Food Applications, R. Rastall, Ed., Woodhead Publishing, Cambridge, UK, 2007. View at Google Scholar
  140. G. Freddi, A. Anghileri, S. Sampaio, J. Buchert, P. Monti, and P. Taddei, “Tyrosinase-catalyzed modification of Bombyx mori silk fibroin: grafting of chitosan under heterogeneous reaction conditions,” Journal of Biotechnology, vol. 125, no. 2, pp. 281–294, 2006. View at Publisher · View at Google Scholar · View at Scopus
  141. B. Dunnewind, T. van Vliet, and R. Orsel, “Effect of oxidative enzymes on bulk rheological properties of wheat flour doughs,” Journal of Cereal Science, vol. 36, no. 3, pp. 357–366, 2002. View at Publisher · View at Google Scholar · View at Scopus
  142. E. Selinheimo, Tyrosinase and laccase as novel crosslinking tools for food biopolymers [Ph.D. thesis], Helsinki University of Technology, Helsinki, Finland, 2008.
  143. E. J. Land, C. A. Ramsden, and P. A. Riley, “Quinone Chemistry and Melanogenesis,” Methods in Enzymology, vol. 378, pp. 88–109, 2004. View at Publisher · View at Google Scholar · View at Scopus
  144. H. Zhao and J. H. Waite, “Coating proteins: structure and cross-linking in fp-1 from the green shell mussel Perna canaliculus,” Biochemistry, vol. 44, no. 48, pp. 15915–15923, 2005. View at Publisher · View at Google Scholar · View at Scopus
  145. S. Bittner, “When quinones meet amino acids: chemical, physical and biological consequences,” Amino Acids, vol. 30, no. 3, pp. 205–224, 2006. View at Publisher · View at Google Scholar · View at Scopus
  146. S. Takasaki and S. Kawakishi, “Formation of protein-bound 3,4-dihydroxyphenylalanine and 5-S-cysteinyl-3,4-dihydroxyphenylalanine as new cross-linkers in gluten,” Journal of Agricultural and Food Chemistry, vol. 45, no. 9, pp. 3472–3475, 1997. View at Google Scholar · View at Scopus
  147. J. G. Jee, S. J. Park, and H. J. Kim, “Tyrosinase-induced cross-linking of tyrosine-containing peptides investigated by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry,” Rapid Communication in Mass Spectrometry, vol. 14, no. 16, pp. 1563–1567, 2000. View at Google Scholar
  148. R. M. Desentis-Mendoza, H. Hernández-Sánchez, A. Moreno et al., “Enzymatic polymerization of phenolic compounds using laccase and tyrosinase from Ustilago maydis,” Biomacromolecules, vol. 7, no. 6, pp. 1845–1854, 2006. View at Publisher · View at Google Scholar · View at Scopus
  149. E. Matuschek and U. Svanberg, “The effect of fruit extracts with polyphenol oxidase (PPO) activity on the in vitro accessibility of iron in high-tannin sorghum,” Food Chemistry, vol. 90, no. 4, pp. 765–771, 2005. View at Publisher · View at Google Scholar · View at Scopus
  150. M. R. Montereali, L. D. Seta, W. Vastarella, and R. Pilloton, “A disposable Laccase-Tyrosinase based biosensor for amperometric detection of phenolic compounds in must and wine,” Journal of Molecular Catalysis B: Enzymatic, vol. 64, no. 3-4, pp. 189–194, 2010. View at Publisher · View at Google Scholar · View at Scopus
  151. J. F. Osma, J. L. Toca-Herrera, and S. Rodríguez-Couto, “Uses of laccases in the food industry,” Enzyme Research, vol. 2010, Article ID 918761, 2010. View at Publisher · View at Google Scholar
  152. G. F. Payne and W.-Q. Sun, “Tyrosinase reaction and subsequent chitosan adsorption for selective removal of a contaminant from a fermentation recycle stream,” Applied and Environmental Microbiology, vol. 60, no. 2, pp. 397–401, 1994. View at Google Scholar · View at Scopus
  153. T. Kuninori, J. Nishiyama, and H. Matsumoto, “Effect of mushroom extract upon the physical properties of dough,” Cereal Chemistry, vol. 53, pp. 420–428, 1976. View at Google Scholar
  154. S. Takasaki, S. Kawakishi, M. Murata, and S. Homma, “Polymerisation of gliadin mediated by mushroom tyrosinase,” LWT—Food Science and Technology, vol. 34, no. 8, pp. 507–512, 2001. View at Publisher · View at Google Scholar · View at Scopus
  155. S. Ito, T. Kato, K. Shinpo, and K. Fujita, “Oxidation of tyrosine residues in proteins by tyrosinase. Formation of protein-bonded 3,4-dihydroxyphenylalanine and 5-S-cysteinyl-3,4-dihydroxyphenylalanine,” Biochemical Journal, vol. 222, no. 2, pp. 407–411, 1984. View at Google Scholar · View at Scopus
  156. C. R. Thalmann and T. Lötzbeyer, “Enzymatic cross-linking of proteins with tyrosinase,” European Food Research and Technology, vol. 214, no. 4, pp. 276–281, 2002. View at Publisher · View at Google Scholar · View at Scopus
  157. R. Lantto, P. Plathin, M. Niemistö, J. Buchert, and K. Autio, “Effects of transglutaminase, tyrosinase and freeze-dried apple pomace powder on gel forming and structure of pork meat,” LWT—Food Science and Technology, vol. 39, no. 10, pp. 1117–1124, 2006. View at Publisher · View at Google Scholar · View at Scopus
  158. R. Lantto, E. Puolanne, K. Kruus, J. Buchert, and K. Autio, “Tyrosinase-aided protein cross-linking: effects on gel formation of chicken breast myofibrils and texture and water-holding of chicken breast meat homogenate gels,” Journal of Agricultural and Food Chemistry, vol. 55, no. 4, pp. 1248–1255, 2007. View at Publisher · View at Google Scholar · View at Scopus
  159. R. Lantto, E. Puolanne, N. Kalkkinen, J. Buchert, and K. Autio, “Enzyme-aided modification of chicken-breast myofibril proteins: effect of laccase and transglutaminase on gelation and thermal stability,” Journal of Agricultural and Food Chemistry, vol. 53, no. 23, pp. 9231–9237, 2005. View at Publisher · View at Google Scholar · View at Scopus
  160. R. Lantto, E. Puolanne, K. Katina, M. Niemistö, J. Buchert, and K. Autio, “Effect of laccase and transglutaminase on the textural and water-binding properties of cooked chicken breast meat gels,” European Food Research and Technology, vol. 225, no. 1, pp. 75–83, 2007. View at Publisher · View at Google Scholar · View at Scopus
  161. G. Seetharam and B. A. Saville, “l-DOPA production from tyrosinase immobilized on zeolite,” Enzyme and Microbial Technology, vol. 31, no. 6, pp. 747–753, 2002. View at Publisher · View at Google Scholar · View at Scopus
  162. G. M. J. Carvalho, T. L. M. Alves, and D. M. G. Freire, “l-DOPA production by immobilized tyrosinase,” Applied Biochemistry and Biotechnology, vol. 84–86, no. 1–9, pp. 791–800, 2000. View at Publisher · View at Google Scholar · View at Scopus
  163. R. Lantto, E. Heine, G. Freddi et al., “Enzymatic modification of wool with tyrosinase and peroxidase,” The Journal of The Textile Institute, vol. 96, no. 2, pp. 109–116, 2005. View at Publisher · View at Google Scholar · View at Scopus
  164. M.-L. Mattinen, R. Lantto, E. Selinheimo, K. Kruus, and J. Buchert, “Oxidation of peptides and proteins by Trichoderma reesei and Agaricus bisporus tyrosinases,” Journal of Biotechnology, vol. 133, no. 3, pp. 395–402, 2008. View at Publisher · View at Google Scholar · View at Scopus
  165. “Burn Dressigns,” in BioMaterials Science: An Introduction to Materials in Medicine, J. B. Kane, R. G. Tompkins, M. L. Yarmush et al., Eds., pp. 360–370, Academic Press, San Diego, Calif, USA, 1996.
  166. K. Y. Lee and D. J. Mooney, “Hydrogels for tissue engineering,” Chemical Reviews, vol. 101, no. 7, pp. 1869–1879, 2001. View at Publisher · View at Google Scholar · View at Scopus
  167. M. E. Marín-Zamora, F. Rojas-Melgarejo, F. García-Cánovas, and P. A. García-Ruiz, “Production of o-diphenols by immobilized mushroom tyrosinase,” Journal of Biotechnology, vol. 139, no. 2, pp. 163–168, 2009. View at Publisher · View at Google Scholar · View at Scopus
  168. M. Guazzaroni, C. Crestini, and R. Saladino, “Layer-by-Layer coated tyrosinase: an efficient and selective synthesis of catechols,” Bioorganic & Medicinal Chemistry, vol. 20, no. 1, pp. 157–166, 2012. View at Publisher · View at Google Scholar · View at Scopus
  169. T. Bozzini, G. Botta, M. Delfino et al., “Tyrosinase and Layer-by-Layer supported tyrosinases in the synthesis of lipophilic catechols with antiinfluenza activity,” Bioorganic & Medicinal Chemistry, vol. 21, no. 24, pp. 7699–7708, 2013. View at Google Scholar