[1] Lješević, M., Gojgić-Cvijović, G., Ieda, T., Hashimoto, S., Nakano, T., Bulatović, S., Ilić, M., and Beškoski, V. (2019) Biodegradation of the aromatic fraction from petroleum diesel fuel by Oerskovia sp. followed by comprehensive GC× GC-TOF MS. J. Hazard. Mater. 363, 227-232.
[2] Besharati, H. (2015) Microbial Remediation of Petroleum Contaminated Soils and the Role of Rhizosphere in Microorganisms Efficiency. Iranian J. Soil Res. 28(3), 573-584.
[3] Logeshwaran, P., Megharaj, M., Chadalavada, S., Bowman, M., and Naidu, R. (2018) Petroleum hydrocarbons (PH) in groundwater aquifers: An overview of environmental fate, toxicity, microbial degradation and risk-based remediation approaches. Environ. Technol. Innov. 10, 175-193.
[4] Silva1, A. S., Jacques, R. J. S., Andreazza, R., Bento, F.M., Roesch, L. F. W., and Camargo, F. A. O. (2013) Properties of catechol 1,2-dioxygenase in the cell free extract and immobilized extract of Mycobacterium fortuitum. Braz. J. Microbiol. 44(1), 291-297.
[5] Nadaf, N. H., and Ghosh, J. S., (2001) Purification and characterization of catechol 1, 2-dioxygenase from Rhodococcus sp. NCIM 2891. Res. J. Environ. Earth Sci. 3(5), 608-613.
[6] Mishra, V. K., and Kumar, N., (2017) Microbial Degradation of Phenol: A Review. J. Water Pollut. Purific. Res. 4(1), 17-22.
[7] Kumar, A., Kumar, S., and Kuma, S., (2005) Biodegradation kinetics of phenol and catechol using Pseudomonas putida MTCC 1194. Biochem. Engin. J. 22, 151-159.
[8] Juhasz, A. L., Naidu, R., (2000) Bioremediation of high molecular weight polycyclic aromatic hydrocarbons: a review of the microbial degradation of benzo(a)pyrene. Int. Biodeterior. Biodegrad. 45, 57–88.
[9] Matera, I., Ferraroni, M., Kolomytseva, M., Golovleva, L., Scozzafava, A., and Briganti, F. (2010) Catechol 1,2-dioxygenase from the Gram-positive Rhodococcus opacus 1CP: Quantitative structure/activity relationship and the crystal structures of native enzyme and catechols adducts. J. Struct. Biol. 170(3), 548-564.
[10] Wang, C, L., You, S, L., and Wang S, L. (2006) Purification and characterization of a novel catechol 1, 2-dioxygenase from Pseudomonas aeruginosa with benzoic acid as a carbon source. Proc. Biochem. 41, 1594-1601.
[11] Milase, R. N. (2015) Purification and characterization of catechol- 1, 2- dioxygenase from Acinetobacter sp. Strain Y64 and Escherichia coli transformants. Submitted to the College of Agriculture, Science and Engineering, School of Life sciences, Discipline of Microbiology, University of KwaZulu-Natal (Westville Campus), in fulfilmentof the degree of Master of Science in Microbiology. 94 p.
[12] Juhasz, A. L., Naidu, R. (2000) Bioremediation of high molecular weight polycyclic aromatic hydrocarbons: a review of the microbial degradation of benzo(a)pyrene. Int. Biodeterior. Biodegrad. 45, 57–88.
[13] Guzik, U., Hupert-Kocurek, K., Sitnik, M., and Wojcieszyńska, D. (2013). High activity catechol 1, 2-dioxygenase from Stenotrophomonas maltophilia strain KB2 as a useful tool in cis, cis-muconic acid production. Anton. Van. Lee. 103(6), 1297-1307.
[14] Bradford, M.M., 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72(1-2), 248-254.
[15] Briganti, F., Pessione, E., Giunta, C., and Scozzafava, A. (1997) Purification, biochemical properties and substrate specificity of a catechol 1,2-dioxygenase from a phenol degrading Acinetobacter radioresistens. Fed. Eur. Biochem. Soci. 416, 61-64.
[16] Di Nardo, G., Tilli, S., Pessione, E., Cavaletto, M., Giunta, C., and Briganti, F. (2004) Structural roles of the active site iron (III) ions in catechol 1,2-dioxygenases and differential secondary structure changes in isoenzymes A and B from Acinetobacter radioresistens S13. Arch. Biochem. Bioph. 431, 79-87.
[17] Nakai, C., Kagamiyama, H., Saeki, Y., and Nozaki, M. (1979) Nonidentical subunits of pyrocatechase from Pseudomonas arvilla C-1. Arch. Biochem. Bioph. 195(1), 12–22.
[18] Sikkema, J., de Bont, J. A., and Poolman, B. (1994) Interactions of cyclic hydrocarbons with biological membranes. J. Biol. Chem. 269 (11), 8022–8028.
[19] Bargeshadi, Z., Pazhang, Y., and Jamei, R. (2019). Effects of organic solvents on the enzyme activity of Subtilisin Carlsberg proteas. J. Mol. Cell. Res. 32(2), 236-246.
[20] Ruiz, D. M., and De Castro, R. E. ( 2007) . Efect of organic solvents on the activity and stability of an extracellular protease secreted by the haloalkaliphilic archaeon Natrialba magadii. J. Ind. Microbiol. Biotechnol. 34, 111-115.
[21] Crowley, J. D., Traynor, D. A., and Weatherburn D. C. (2000) Enzymes and proteins containing manganese: An overview. Met. Ions Biol. Syst. 37, 209-278.
[22] Shirdel, S.A., and Khalifeh K. (2019). Thermodynamics of protein folding: methodology, data analysis and interpretation of data, Eur. Biophys. J. 48, 305–316.