References
- Anthoni, J., Lionneton, F., Wieruszeski, J. M., Magdalou, J., Engasser, J. M., Chebil, L., Humeau, C., & Ghoul, M. (2008). Investigation of enzymatic oligomerization of rutin. Rasayan Journal of Chemistry, 1, 718–731.
- Araújo, M., Pimentel, F. B., Alves, R. C., & Oliveira, M. B. P. P. (2015). Phenolic compounds from olive mill wastes: Health effects, analytical approach and application as food antioxidants. Trends in Food Science & Technology, 45(2), 200–211. https://doi.org/https://doi.org/10.1016/j.tifs.2015.06.010
- Awasthi, M., Jaiswal, N., Singh, S., Pandey, V. P., & Dwivedi, U. N. (2015). Molecular docking and dynamics simulation analyses unraveling the differential enzymatic catalysis by plant and fungal laccases with respect to lignin biosynthesis and degradation. Journal of Biomolecular Structure & Dynamics, 33(9), 1835–1849. https://doi.org/https://doi.org/10.1080/07391102.2014.975282
- Baldrian, P. (2004). Purification and characterization of laccase from the white-rot fungus Daedalea quercina and decolorization of synthetic dyes by the enzyme. Applied Microbiology and Biotechnology, 63(5), 560–563. https://doi.org/https://doi.org/10.1007/s00253-003-1434-0
- Bilal, M., Adeel, M., Rasheed, T., Zhao, Y., & Iqbal, H. M. N. (2019). Emerging contaminants of high concern and their enzyme-assisted biodegradation—A review. Environment International, 124, 336–353. https://doi.org/https://doi.org/10.1016/j.envint.2019.01.011
- Bruno, F. F., Trotta, A., Fossey, S., Nagarajan, S., Nagarajan, R., Samuelson, L. A., & Kumar, J. (2010). Enzymatic synthesis and characterization of polyquercetin. Journal of Macromolecular Science, Part A, 47(12), 1191–1196. https://doi.org/https://doi.org/10.1080/10601325.2010.518839
- Cambria, M. T., Gullotto, D., Garavaglia, S., & Cambria, A. (2012). In silico study of structural determinants modulating the redox potential of Rigidoporus lignosus and other fungal laccases. Journal of Biomolecular Structure & Dynamics, 30(1), 89–101. https://doi.org/https://doi.org/10.1080/07391102.2012.674275
- Cardinali, A., Cicco, N., Linsalata, V., Minervini, F., Pati, S., Pieralice, M., Tursi, N., & Lattanzio, V. (2010). Biological activity of high molecular weight phenolics from olive mill wastewater. Journal of Agricultural and Food Chemistry, 58(15), 8585–8590. https://doi.org/https://doi.org/10.1021/jf101437c
- Chen, Y., Zhao, L., & Jiang, J. (2017). The naphthoate-modifying Cu2+-detective Bodipy sensors with the fluorescent ON-OFF performance unaffected by molecular configuration. Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy, 175, 269–275. https://doi.org/https://doi.org/10.1016/j.saa.2016.12.034
- Conceição, J. C. S., Dias, H. J., Peralva, C. M. S., Crotti, A. E. M., da Rocha Pita, S. S., & de Oliveira Silva, E. (2020). Phenolic compound biotransformation by Trametes versicolor ATCC 200801 and molecular docking studies. Applied Biochemistry and Biotechnology, 190(4), 1498–1511. https://doi.org/https://doi.org/10.1007/s12010-019-03191-y
- Dec, J., & Bollag, J. M. (1990). Detoxification of substituted phenols by oxidoreductive enzymes through polymerization reactions. Archives of Environmental Contamination and Toxicology, 19(4), 543–550. https://doi.org/https://doi.org/10.1007/BF01059073
- Desentis-Mendoza, R. M., Hernández-Sánchez, H., Moreno, A., Rojas del C, E., Chel-Guerrero, L., Tamariz, J., & Jaramillo-Flores, M. E. (2006). Enzymatic polymerization of phenolic compounds using laccase and tyrosinase from Ustilago maydis. Biomacromolecules, 7(6), 1845–1854. https://doi.org/https://doi.org/10.1021/bm060159p
- Dicésare, N., Belletête, M., Leclerc, M., & Durocher, G. (1999). HF/3-21G* ab initio calculations on methoxy-substituted bithiophenes. Journal of Molecular Structure: Theochem, 467(3), 259–273. https://doi.org/https://doi.org/10.1016/S0166-1280(99)00002-0
- Duran, N., & Esposito, E. (2000). Potential applications of oxidative enzymes and phenoloxidase-like compounds in wastewater and soil treatment: A review. Applied Catalysis B: Environmental, 28(2), 83–99. https://doi.org/https://doi.org/10.1016/S0926-3373(00)00168-5
- Edwards, W., Bownes, R., Leukes, W. D., Jacobs, E. P., Sanderson, R., Rose, P. D., & Burton, S. G. (1999). A capillary membrane bioreactor using immobilized polyphenol oxidase for the removal of phenols from industrial effluents. Enzyme and Microbial Technology, 24(3–4), 209–217. https://doi.org/https://doi.org/10.1016/S0141-0229(98)00110-0
- Gao, X., Huang, S., Dong, P., Wang, C., Hou, J., Huo, X., Zhang, B., Ma, T., & Ma, X. (2016). Horseradish peroxidase (HRP): A tool for catalyzing the formation of novel bicoumarins. Catalysis Science & Technology, 6(10), 3585–3593. https://doi.org/https://doi.org/10.1039/C5CY01682G
- Garcia-Molina, F., Hiner, A. N. P., Fenoll, L. G., Rodriguez-Lopez, J. N., Garcia-Ruiz, P. A., Garcia-Canovas, F., & Tudela, J. (2005). Mushroom tyrosinase: Catalase activity, inhibition, and suicide inactivation. Journal of Agricultural and Food Chemistry, 53(9), 3702–3709. https://doi.org/https://doi.org/10.1021/jf048340h
- González-Sánchez, M. I., Laurenti, M., Rubio-Retama, J., Valero, E., & Lopez-Cabarcos, E. (2011). Fluorescence decrease of conjugated polymers by the catalytic activity of horseradish peroxidase and its application in phenolic compounds detection. Biomacromolecules, 12(4), 1332–1338. https://doi.org/https://doi.org/10.1021/bm200091m
- Güreşir, M., Aktaş, N., & Tanyolaç, A. (2005). Influence of reaction conditions on the rate of enzymic polymerization of pyrogallol using laccase. Process Biochemistry, 40(3–4), 1175–1182. https://doi.org/https://doi.org/10.1016/j.procbio.2004.04.007
- Hanoian, P., Liu, C. T., Hammes-Schiffer, S., & Benkovic, S. (2015). Perspectives on electrostatics and conformational motions in enzyme catalysis. Accounts of Chemical Research, 48(2), 482–489. https://doi.org/https://doi.org/10.1021/ar500390e
- Hongyan, L., Zexiong, Z., Shiwei, X., He, X., Yinian, Z., Haiyun, L., & Zhongsheng, Y. (2019). Study on transformation and degradation of bisphenol A by Trametes versicolor laccase and simulation of molecular docking. Chemosphere, 224, 743–750. https://doi.org/https://doi.org/10.1016/j.chemosphere.2019.02.143
- Hosny, M., & Rosazza, J. P. N. (2002). Novel oxidations of (+)-catechin by horseradish peroxidase and laccase. Journal of Agricultural and Food Chemistry, 50(20), 5539–5545. https://doi.org/https://doi.org/10.1021/jf020503j
- Ikeda, R., Sugihara, J., Uyama, H., & Kobayashi, S. (1998). Enzymatic oxidative polymerization of 4-hydroxybenzoic acid derivatives to poly(phenylene oxide)s. Polymer International, 47(3), 295–301. https://doi.org/https://doi.org/10.1002/(SICI)1097-0126(199811)47:3<295::AID-PI7>3.0.CO;2-W
- Ikehata, K., & Nicell, J. A. (2000). Characterization of tyrosinase for the treatment of aqueous phenols. Bioresource Technology, 74(3), 191–199. https://doi.org/https://doi.org/10.1016/S0960-8524(00)00025-0
- Khan, I. A., & Ali, R. (1986). Antigenicity, catalytic activity and conformation of Agaricus bisporus tyrosinase: interaction of conformation-directed antibodies with the native and irradiated enzyme . Journal of Biochemistry, 99(2), 445–452. https://doi.org/https://doi.org/10.1093/oxfordjournals.jbchem.a135498
- Kim, Y. J., & Nicell, J. A. (2006). Impact of reaction conditions on the laccase-catalyzed conversion of bisphenol A. Bioresource Technology, 97(12), 1431–1442. https://doi.org/https://doi.org/10.1016/j.biortech.2005.06.017
- Kobayashi, S., Kurioka, H., & Uyama, H. (1996). Enzymatic synthesis of a soluble polyphenol derivative from 4,4′-biphenyldiol. Macromolecular Rapid Communications, 17(8), 503–508. https://doi.org/https://doi.org/10.1002/marc.1996.030170802
- Kobayashi, S., Uyama, H., & Kimura, S. (2001). Enzymatic polymerization. Chemical Reviews, 101(12), 3793–3818. https://doi.org/https://doi.org/10.1021/cr990121l
- Koroleva, O. V., Gavrilova, V. P., Yavmetdinov, I. S., Shleev, S. V., & Stepanova, E. V. (2001). Isolation and study of some properties of laccase from the Basidiomycetes Cerrena maxima. Biochemistry. Biokhimiia, 66(6), 618–622.
- Kurisawa, M., Chung, J. E., Kim, Y. J., Uyama, H., & Kobayashi, S. (2003). Amplification of antioxidant activity and xanthine oxidase inhibition of catechin by enzymatic polymerization. Biomacromolecules, 4(3), 469–471. https://doi.org/https://doi.org/10.1021/bm034012z
- Kurniawati, S., & Nicell, J. A. (2008). Characterization of Trametes versicolor laccase for the transformation of aqueous phenol. Bioresource Technology, 99(16), 7825–7834. https://doi.org/https://doi.org/10.1016/j.biortech.2008.01.084
- Litescu, S. C., Eremia, S., & Radu, G. L. (2010). Biosensors for the determination of phenolic metabolites. Advances in Experimental Medicine and Biology, 698, 234–240. https://doi.org/https://doi.org/10.1007/978-1-4419-7347-4_17
- Liu, W. Y., Zou, C. M., Hu, J. H., Xu, Z. J., Si, L. Q., Liu, J. J., & Huang, J. G. (2020). Kinetic characterization of tyrosinase-catalyzed oxidation of four polyphenols. Current Medical Science, 40(2), 239–248. https://doi.org/https://doi.org/10.1007/s11596-020-2186-0
- Mahfoudi, R., Djeridane, A., Benarous, K., Gaydou, E. M., & Yousfi, M. (2017). Structure-activity relationships and molecular docking of thirteen synthesized flavonoids as horseradish peroxidase inhibitors. Bioorganic Chemistry, 74, 201–211. https://doi.org/https://doi.org/10.1016/j.bioorg.2017.08.001
- Marszałek, K., Krzyżanowska, J., Woźniak, Ł., & Skąpska, S. (2017). Kinetic modelling of polyphenol oxidase, peroxidase, pectin esterase, polygalacturonase, degradation of the main pigments and polyphenols in beetroot juice during high pressure carbon dioxide treatment. LWT—Food Science and Technology, 85, 412–417. https://doi.org/https://doi.org/10.1016/j.lwt.2016.11.018
- Mazzafera, P., & Robinson, S. P. (2000). Characterization of polyphenol oxidase in coffee. Phytochemistry, 55(4), 285–296. https://doi.org/https://doi.org/10.1016/S0031-9422(00)00332-0
- Mehra, R., Muschiol, J., Meyer, A. S., & Kepp, K. P. (2018). A structural-chemical explanation of fungal laccase activity. Scientific Report-UK, 8, 17285.
- Mezei, P. D., & Csonka, G. I. (2015). Unified picture for the conformation and stabilization of the O-glycosidic linkage in glycopeptide model structures. Structural Chemistry, 26(5–6), 1367–1376. https://doi.org/https://doi.org/10.1007/s11224-015-0666-9
- Mo, D., Zeng, G., Yuan, X., Chen, M., Hu, L., Li, H., Wang, H., Xu, P., Lai, C., Wan, J., Zhang, C., & Cheng, M. (2018). Molecular docking simulation on the interactions of laccase from Trametes versicolor with nonylphenol and octylphenol isomers. Bioprocess and Biosystems Engineering, 41(3), 331–343. https://doi.org/https://doi.org/10.1007/s00449-017-1866-z
- Molitor, C., Mauracher, S. G., & Rompel, A. (2016). Aurone synthase is a catechol oxidase with hydroxylase activity and provides insights into the mechanism of plant polyphenol oxidases. Proceedings of the National Academy of Sciences, 113(13), E1806–1815. https://doi.org/https://doi.org/10.1073/pnas.1523575113
- Oliver, S., Vittorio, O., Cirillo, G., & Boyer, C. (2016). Enhancing the therapeutic effects of polyphenols with macromolecules. Polymer Chemistry, 7(8), 1529–1544. https://doi.org/https://doi.org/10.1039/C5PY01912E
- Paulo, F., & Santos, L. (2020). Deriving valorization of phenolic compounds from olive oil by-products for food applications through microencapsulation approaches: A comprehensive review. Critical Reviews in Food Science and Nutrition, 11, 1–26.
- Pinheiro, V. E., Michelin, M., Vici, A. C., de Almeida, P. Z., & Teixeira de Moraes Polizeli, MdL. (2020). Trametes versicolor laccase production using agricultural wastes: A comparative study in erlenmeyer flasks, bioreactor and tray. Bioprocess and Biosystems Engineering, 43(3), 507–514. https://doi.org/https://doi.org/10.1007/s00449-019-02245-z
- Pogni, R., Baratto, M. C., Sinicropi, A., & Basosi, R. (2015). Spectroscopic and computational characterization of laccases and their substrate radical intermediates. Cellular and Molecular Life Sciences, 72(5), 885–896. https://doi.org/https://doi.org/10.1007/s00018-014-1825-7
- Roberts, J. J., Naudiyal, P., Lim, K. S., Poole-Warren, L. A., & Martens, P. J. (2016). A comparative study of enzyme initiators for crosslinking phenol-functionalized hydrogels for cell encapsulation. Biomaterials Research, 20, 30–42. https://doi.org/https://doi.org/10.1186/s40824-016-0077-z
- Robles, A., Lucas, R., de Cienfuegos, G. A., & Gálvez, A. (2000). Phenol-oxidase (laccase) activity in strains of the hyphomycete Chalara paradoxa isolated from olive mill wastewater disposal ponds. Enzyme and Microbial Technology, 26, 484–490. https://doi.org/https://doi.org/10.1016/S0141-0229(99)00197-0
- Rodakiewicz-Nowak, J. (2000). Phenols oxidizing enzymes in water-restricted media. Topics in Catalysis, 11/12(1/4), 419–434. https://doi.org/https://doi.org/10.1023/A:1027291629302
- Rueda, N., dos Santos, J. C. S., Ortiz, C., Torres, R., Barbosa, O., Rodrigues, R. C., Berenguer-Murcia, Á., & Fernandez-Lafuente, R. (2016). Chemical modification in the design of immobilized enzyme biocatalysts: Drawbacks and opportunities. Chemical Record (New York, N.Y.), 16(3), 1436–1455. https://doi.org/https://doi.org/10.1002/tcr.201600007
- Sánchez-Ferrer, Á., Neptuno Rodríguez-López, J., García-Cánovas, F., & García-Carmona, F. (1995). Tyrosinase: A comprehensive review of its mechanism. Biochimica et Biophysica Acta (BBA)—Protein Structure and Molecular Enzymology, 1247(1), 1–11. https://doi.org/https://doi.org/10.1016/0167-4838(94)00204-T
- Sarkar, S., Banerjee, A., Chakraborty, N., Soren, K., Chakraborty, P., & Bandopadhyay, R. (2020). Structural-functional analyses of textile dye degrading azoreductase, laccase and peroxidase: A comparative in silico study. Electronic Journal of Biotechnology, 43, 48–54. https://doi.org/https://doi.org/10.1016/j.ejbt.2019.12.004
- Shalit, H., Dyadyuk, A., & Pappo, D. (2019). Selective oxidative phenol coupling by iron catalysis. The Journal of Organic Chemistry, 84(4), 1677–1686. https://doi.org/https://doi.org/10.1021/acs.joc.8b03084
- Shleev, S., Reimann, C. T., Serezhenkov, V., Burbaev, D., Yaropolov, A. I., Gorton, L., & Ruzgas, T. (2006). Autoreduction and aggregation of fungal laccase in solution phase: Possible correlation with a resting form of laccase. Biochimie, 88(9), 1275–1285. https://doi.org/https://doi.org/10.1016/j.biochi.2006.02.007
- Shoda, S. I., Uyama, H., Kadokawa, J. I., Kimura, S., & Kobayashi, S. (2016). Enzymes as green catalysts for precision macromolecular synthesis. Chemical Reviews, 116(4), 2307–2413. https://doi.org/https://doi.org/10.1021/acs.chemrev.5b00472
- Solná, R., & Skládal, P. (2005). Amperometric flow-injection determination of phenolic compounds using a biosensor with immobilized laccase, peroxidase and tyrosinase. Electroanalysis, 17(23), 2137–2146. https://doi.org/https://doi.org/10.1002/elan.200403343
- Solomon, E. I., Augustine, A. J., & Yoon, J. (2008). O2 Reduction to H2O by the multicopper oxidases. Dalton Transactions, 30(30), 3921–3932. https://doi.org/https://doi.org/10.1039/b800799c
- Stadlmair, L. F., Letzel, T., & Graßmann, J. (2018). Monitoring enzymatic degradation of emerging contaminants using a chip-based robotic nano-ESI-MS tool. Analytical and Bioanalytical Chemistry, 410(1), 27–32. https://doi.org/https://doi.org/10.1007/s00216-017-0729-4
- Torres, E., Bustos-Jaimes, I., & Le Borgne, S. (2003). Potential use of oxidative enzymes for the detoxification of organic pollutants. Applied Catalysis B: Environmental, 46(1), 1–15. https://doi.org/https://doi.org/10.1016/S0926-3373(03)00228-5
- Wang, Z. Q., Song, Q. Y., Su, J. C., Tang, W., Song, J. G., Huang, X. J., An, J., Li, Y. L., Ye, W. C., & Wang, Y. (2020). Caffeic acid oligomers from Mesona chinensis and their in vitro antiviral activities. Fitoterapia , 144, 104603https://doi.org/https://doi.org/10.1016/j.fitote.2020.104603
- Wu, Y., Taylor, K. E., Biswas, N., & Bewtra, J. K. (1998). A model for the protective effect of additives on the activity of horseradish peroxidase in the removal of phenol. Enzyme and Microbial Technology, 22(5), 315–322. https://doi.org/https://doi.org/10.1016/S0141-0229(97)00197-X
- Xu, P., Uyama, H., Whitten, J. E., Kobayashi, S., & Kaplan, D. L. (2005). Peroxidase-catalyzed in situ polymerization of surface orientated caffeic acid. Journal of the American Chemical Society, 127(33), 11745–11753. https://doi.org/https://doi.org/10.1021/ja051637r
- Yan, Q., Tang, X., Zhang, B., Wang, C., Deng, S., Ma, X., Wang, C., Li, D., Huang, S., & Dong, P. (2019). Biocatalytic oxidation of flavone analogues mediated by general biocatalysts: Horseradish peroxidase and laccase. RSC Advances, 9(23), 13325–13331. https://doi.org/https://doi.org/10.1039/C9RA00470J
- Yang, F., Yu, P. Y., Zhao, J., Zhao, Y., & Wang, J. P. (2015). Intermolecular hydrogen bonding structural dynamics in ethylene glycol by femtosecond nonlinear infrared spectroscopy. Acta Physico-Chimica Sinica, 31, 1275–1282.
- Yu, Q., Fan, L., & Duan, Z. (2019). Five individual polyphenols as tyrosinase inhibitors: Inhibitory activity, synergistic effect, action mechanism, and molecular docking. Food Chemistry, 297, 124910https://doi.org/https://doi.org/10.1016/j.foodchem.2019.05.184
- Zhu, Z., Luo, W., & Sun, D.-W. (2020). Effects of liquid nitrogen quick freezing on polyphenol oxidase and peroxide activities, cell water states and epidermal microstructure of wolfberry. LWT, 120, 108923. https://doi.org/https://doi.org/10.1016/j.lwt.2019.108923
- Zwane, R. E., Parker, A., Kudanga, T., Davids, L. M., & Burton, S. G. (2012). Novel, biocatalytically produced hydroxytyrosol dimer protects against ultraviolet-induced cell death in human immortalized keratinocytes. Journal of Agriculatural and Food Chemistry, 60(46), 11509–11517. https://doi.org/https://doi.org/10.1021/jf300883h