Properties of catechol 2,3-dioxygenase from crude extract of Stenotrophomonas maltophilia strain KB2 immobilized in calcium alginate hydrogels

Biochemical Engineering Journal

Volumn 66, Issue , 2012, Pages 1-7

  Wojcieszyńska, Danuta ^a   Hupert Kocurek, Katarzyna ^a   Jankowska, Anna ^a   Guzik, Urszula ^a  

^a UNIVERSITY OF SILESIA   (Poland)

Author keywords

Biodegradation; Catechol 2,3 dioxygenase; Immobilization; Kinetic parameters; Stenotrophomonas; Substrate inhibition

Indexed keywords

4-METHYLCATECHOL; ALGINATE HYDROGELS; CALCIUM ALGINATE; CATECHOL 2,3-DIOXYGENASE; CRUDE EXTRACT; DIOXYGENASES; FREE ENZYME; IMMOBILIZED ENZYME; OPTIMUM TEMPERATURE; SOLUBLE ENZYMES; STENOTROPHOMONAS; STENOTROPHOMONAS MALTOPHILIA; STORAGE STABILITY; STRUCTURAL RIGIDITY; SUBSTRATE INHIBITION;

BIODEGRADATION; BIOREMEDIATION; DETOXIFICATION; ENZYME ACTIVITY; ENZYME IMMOBILIZATION; KETONES; KINETIC PARAMETERS; PHENOLS; PROTEINS; RADIOACTIVE WASTE VITRIFICATION;

ENZYME INHIBITION;

3 METHYLCATECHOL; 3,5 DICHLOROCATECHOL; 4 METHYLCATECHOL; 4,5 DICHLOROCATECHOL; CALCIUM ALGINATE; CATECHOL 2,3 DIOXYGENASE; CATECHOL DERIVATIVE; COPPER SULFATE; HYDROGEN PEROXIDE; HYDROQUINONE; SODIUM AZIDE; TETRACHLOROHYDROQUINONE; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL STRAIN; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME IMMOBILIZATION; ENZYME INACTIVATION; ENZYME INHIBITION; ENZYME STABILITY; ENZYME STRUCTURE; HYDROGEL; NONHUMAN; PH; PRIORITY JOURNAL; REACTION OPTIMIZATION; STENOTROPHOMONAS MALTOPHILIA; TEMPERATURE DEPENDENCE;

STENOTROPHOMONAS; STENOTROPHOMONAS MALTOPHILIA;

EID: 84860695543     PISSN: 1369703X     EISSN: 1873295X     Source Type: Journal    
DOI: 10.1016/j.bej.2012.04.008     Document Type: Article

References (52)

1. Albaugh C.E. Degradation of monoaromatic compounds by an aerobic halotolerant alkaliphilic bacterium. Master of Science Thesis 2005, Washington State University, Washington.
2. Briganti F., Pessione E., Giunta C., Mazzoli R., Scozzafava A. Purification and catalytic properties of two catechol 1,2-dioxygenase isozymes from benzoate-grown cells of Acinetobacter radioresisten. J. Protein Chem. 2000, 19:709-716.
3. Greń I., Wojcieszyńska D., Guzik U., Perkosz M., Hupert-Kocurek K. Enhanced biotransformation of mononitrophenols by Stenotrophomonas maltophilia KB2 in the presence of aromatic compounds of plant origin. World J. Microbiol. Biotechnol. 2010, 26:289-295.
4. Guzik U., Greń I., Wojcieszyńska D., Labużek S. Isolation and characterization of a novel strain of Stenotrophomonas maltophilia possessing various dioxygenases for monocyclic hydrocarbon degradation. Braz. J. Microbiol. 2009, 40:285-291.
5. Guzik U., Greń I., Hupert-Kocurek K., Wojcieszyńska D. Catechol 1,2-dioxygenase from the new aromatic compounds - degrading Pseudomonas putida strain N6. Int. Biodeterior. Biodegrad. 2011, 65:504-512.
6. Vaillancourt F.H., Bolin J.T., Eltis L.D. The ins and outs of ring-cleaving dioxygenases. Crit. Rev. Biochem. Mol. Biol. 2006, 41:241-267.
7. Ch.L.Wang, You S.L., Wang S.L. Purification and characterization of a novel catechol 1,2-dioxygenase from Pseudomonas aeruginosa with benzoic acid as a carbon source. Process Biochem. 2006, 41:1594-1601.
8. Wojcieszyńska D., Guzik U., Greń I., Perkosz M., Hupert-Kocurek K. Induction of aromatic ring - cleavage dioxygenases in Stenotrophomonas maltophilia strain KB2 in cometabolic systems. World J. Microbiol. Biotechnol. 2011, 27:805-811.
9. Chae J.Ch., Kim E., Bini E., Zylstra G.J. Comparative analysis of the catechol 2,3-dioxygenase gene locus in thermoacidophilic archeon Sulfolobus solfataricus strain 98/2, Biochem. Biophys. Res. Commun. 2007, 357:815-819.
10. Fernandez-Lafuente R., Guisan J.M., Ali S., Cowan D. Immobilization of functionally unstable catechol 2,3-dioxygenase greatly improves operational stability. Enzyme Microb. Technol. 2000, 26:568-573.
11. Kalogeris E., Sanakis Y., Mamma D., Christakopoulos P., Kekos D., Stamatis H. Properties of catechol 1,2-dioxygenase from Pseudomonas putida immobilized in calcium alginate hydrogels. Enzyme Microb. Technol. 2006, 39:1113-1121.
12. Bertini I., Briganti F., Scozzafava A. Aliphatic and aromatic inhibitors binding to the active site of catechol 2,3-dioxygenase from Pseudomonas putida mt-2. FEBS Lett. 1994, 242:56-60.
13. Kaschabek S.R., Kasberg T., Muller D., Mars A.E., Janssen D.B., Reineke W. Degradation of chloroaromatics: purification and characterization of a novel type of chlorocatechol 2,3-dioxygenase of Pseudomonas putida GJ31. J. Bacteriol. 1998, 180:296-302.
14. Milo R.E., Duffner F.M., Muller R. Catechol 2,3-dioxygenase from the thermophilic, phenol-degrading Bacillus thermoleovorans strain A2 has unexpected low thermal stability. Extremophiles 1999, 3:185-190.
15. Palaniandavar M., Mayilmurugan R. Mononuclear nan-heme iron (IIII complexes as functional models for catechol dioxygenases. C.R. Chim. 2007, 10:366-379.
16. Que L., Widom J., Crawford R.L. 3,4-Dihydroxyphenylacetate 2,3-dioxygenase. A manganese (II) dioxygenase from Bacillus brevis. J. Biol. Chem. 1981, 256:10941-10944.
17. Hassett D.J., Ochsner U.A., Groce S.L., Parvatiyar K., Ma J.-F., Lipscomb J.D. Hydrogen peroxide sensitivity of catechol 2,3-dioxygenase: a cautionary note on use of xylE reporter fusions under aerobic conditions. Appl. Environ. Microbiol. 2000, 66:4119-4123.
18. Bartels I., Knackmuss H.-J., Reineke W. Suicide inactivation of catechol 2,3-dioxygenase from Pseudomonas putida mt-2 by 3-halocatechols. Appl. Environ. Microbiol. 1984, 47:500-505.
19. Klečka G.M., Gibson D.T. Inhibition of catechol 2,3-dioxygenase from Pseudomonas putida by 3-chlorocatechol. Appl. Environ. Microbiol. 1981, 41:1159-1165.
20. çil M., Böyükbayram A.E., Kiralp S., Toppare L., Yagci Y. Various application of immobilized glucose oxidase and polyphenol oxidase in a conductiong polymer matrix. Int. J. Biol. Macromol. 2007, 41:49-55.
21. Kara F., Demirel G., Tümtürk H. Immobilization of urease by Rusing chitosan-alginate and poly(acrylamide-co-acrylic acid/κ-carrageenan supports. Bioprocess. Biosyst. Eng. 2006, 29:207-211.
22. Tümtürk H., Karaca N., Demirel G., Sahin F. Preparation and application of poly(N,N-dimethylacrylamide-co-acrylamide) and poly(N-isopropylacrylamide-co-acrylamide)/κ-Carrageenan hydrogels for immobilization of lipase. Int. J. Biol. Macromol. 2007, 40:281-285.
23. Fernandez-Lafuente R. Stabilization of multimeric enzymes: strategies to prevent subunit dissociation. Enzyme Microb. Technol. 2009, 45:405-418.
24. Mateo C., Palomo J.M., Fernandez-Lorente G., Guisan J.M., Fernendez-Lafuente R. Improvoment of enzyme activity, stability and selectivity via immobilization techniques. Enzyme Microb. Technol. 2007, 40:1451-1463.
25. Wojcieszyńska D., Hupert-Kocurek K., Greń I., Guzik U. High activity catechol 2,3-dioxygenase from the cresols-degrading Stenotrophomonas maltophilia strain KB2. Int. Biodeterior. Biodegrad. 2011, 65:853-858.
26. Cowan D.A., Fernandez-Lafuente R. Enhancing the functional properties of thermophilic enzymes by chemical modification and immobilization. Enzyme Microb. Technol. 2011, 49:326-346.
27. Garcia-Galan C., Berenguer-Murcia A., Fernandez-Lafuente R., Rodrigues R.C. Potential of different enzyme immobilization strategies to improve enzyme performance. Adv. Synth. Catal. 2011, 353:2885-2904.
28. Riaz A., Qader S.A.U., Anwar A., Iqbal S. Immobilization of a termostable α-amylase on calcium alginate beads from Bacillus subtilis KIBGE-HAR. Aust. J. Basic Appl. Sci. 2009, 3:2883-2887.
29. Brady D., Jordaan J. Advances in enzyme immobilization. Biotechnol. Lett. 2009, 31:1639-1650.
30. Won K., Kim S., Kim K-J., Park H.W., Moon S-J. Optimization of lipase entrapment in Ca-alginate gel beads. Process Biochem. 2005, 40:2149-2154.
31. Bradford M.M. A rapid and sensitive method of the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-258.
32. Bayly R.C., Dagley S., Gibson D.T. The metabolism of cresols by species of Pseudomonas. Biochem. J. 1966, 101:293-301.
33. Heiss G., Muller C., Altenbuchner J., Stolz A. Analysis of a new dimeric extradiol dioxygenase from a naphthalenesulfonate-degrading sphingomonad. Microbiology 1997, 143:1691-1699.
34. Horvath R.S. Co-metabolism of methyl- and chloro-substituted catechols by an Achromobacter sp. possessing a new meta-cleaving oxygenase. Biochem. J. 1970, 119:871-876.
35. Kolvenbach B.A., Lenz M., Bendorf D., Rapp E., Fousek J., Vlcek C., Schaffer A., Gabriel F.L.P., Kohler H.-P.E., Corvini P.F.X. Purification and characterization of hydroquinone dioxygenase from Sphingomonas sp. strain TTNP3. AMB Express 2011, 1:1-8.
36. Spain J.C., Gibson D.T. Pathway for biodegradation of p-nitrophenol in a Moraxella sp. Appl. Environ. Microbiol. 1991, 57:812-819.
37. Wallis M.G., Chapman S.K. Isolation and partial characterization of an extradiol non- haem iron dioxygenase which preferentially cleaves 3-methylcatechol. Biochem. J. 1990, 266:605-609.
38. Hollender J., Hopp J., Dott W. Cooxidation of chloro- and methylphenols by Alcaligenes xylosoxidans JH1. World J. Microbiol. Biotechnol. 2000, 16:445-450.
39. Ho K.L., Chen Y.Y., Lee D.J. Functional consortia for cresol- degrading activated sludge: toxicity-to-extinction approach. Bioresour. Technol. 2010, 101:9000-9005.
40. Arica M.Y., Bayramoglu G., Biçak N. Characterisation of tyrosinase immobilized onto spacer-arm attache glycidyl methacrylate-based reactive microbeads. Process Biochem. 2004, 39:2007-2017.
41. Junca H., Plumeier I., Hecht H.J., Pieper D.H. Difference in kinetic behavior of catechol 2,3-dioxygenase variants from a polluted environment. Microbiology 2004, 150:4181-4187.
42. Taqieddin E., Amiji M. Enzyme immobilization in novel alginate-chitosan core-shell microcapsules. Biomaterials 2004, 25:1937-1945.
43. Knezevic Z., Bobic S., Milutinovic A., Obradovic B., Mojovic L., Bugarski B. Alginate-immobilized lipase by electrostatic extrusion for the purpose of palm oil hydrolysis in lecithin/isooctane system. Process Biochem. 2002, 38:313-318.
44. Shafei M.S., Allam R.F. Production and immobilization of partially purified lipase from Penicillium chrysogenum. Malays. J. Microbiol. 2010, 6:196-202.
45. Takeo M., Nishimura M., Shirai M., Takahashi H., Kitamura Ch., Negoro S. Purification and characterization of catechol 2,3-dioxygenase from aniline degradation pathway of Acinetobacter sp. YAA and its mutant enzyme, which resists substrate inhibition. J. Biosci. Bioeng. 2007, 71:1668-1675.
46. Iwaki M., Nozaki M. Immobilization of metapyrocatechase and its properties in comparison with the soluble enzyme. J. Biochem. 1982, 91:1549-1553.
47. Kita A., Kita S., Fujisawa I., Inaka K., Ishida T., Horiike K., Nozaki M., Miki K. An archetypical extradiol-cleaving catecholic dioxygenase: the crystal structure of catechol 2,3-dioxygenase (metapyrocatechase) from Pseudomonas putida mt-2. Structure 1999, 7:25-34.
48. Nordin K., Unell M., Jansson J.K. Novel 4-chlorophenol degradation gene cluster and degradation route via hydroxyquinol in Arthrobacter chlorophenolicus A6. Appl. Environ. Microbiol. 2005, 71:6538-6544.
49. Vaillancourt F.H., Han S., Fortin P.D., Bolin J.T., Eltis L.D. Molecular basis for the stabilization and inhibition of 2,3-dihydroxybiphenyl 1,2-dioxygenase by t-butanol. J. Biol. Chem. 1998, 273:34887-34895.
50. Ha Y.M., Jung Y.H., Kwon D.Y., Kim Y., Kim C.-K., Min K.H. Reaction characteristics of 4-methylcatechol 2,3-dioxygenase from Pseudomonas putida SU10. J. Microbiol. Biotechnol. 2000, 10:35-42.
51. Thomas D., Bourdillon C., Broun G., Kernevez J.P. Kinetic behavior of enzymes in artificial membranes. Inhibition and reversibility effects. Biochemistry 1974, 14:2995-3000.
52. Abian O., Wilson L., Mateo C., Fernandez-Lorente G., Palomo J.M., Fernandez-Lafuente R., Guisan J.M., Re D., Tam A., Daminatti M. Preparation of artificial hyper-hydrophilic micro-environments (polymeric salts) surrounding enzyme molecules. New enzyme derivatives to be used in any reaction medium. Mol. Catal. B: Enzym. 2002, 19-20:295-303.