Purification and characterization of a psychrophilic catalase from Antarctic Bacillus

Canadian Journal of Microbiology

Volumn 54, Issue 10, 2008, Pages 823-828

  Wang, Wei ^a   Sun, Mi ^a   Liu, Wanshun ^b   Zhang, Bin ^a  

^a YELLOW SEA FISHERIES RESEARCH INSTITUTE   (China)

^b OCEAN UNIVERSITY OF CHINA   (China)

Author keywords

Activation energy (Ea); Kcat Km; Psychrophilic monofunctional catalase; Purification; Thermostability

Indexed keywords

AMINES; BACTERIOLOGY; CHEMICAL ACTIVATION; ENZYMES; PLANTS (BOTANY); PURIFICATION; SEAWATER;

BACILLUS SP.; CATALYTIC EFFICIENCIES; KCAT/KM; LOW TEMPERATURES; MERCAPTOETHANOL; MESOPHILIC; MONOFUNCTIONAL CATALASES; OPTIMAL ACTIVITIES; PH RANGES; PSYCHROPHILIC MONOFUNCTIONAL CATALASE; THERMOSTABILITY;

ACTIVATION ENERGY;

AZIDE; CATALASE; HYDROGEN PEROXIDE; HYDROXYLAMINE; MERCAPTOETHANOL; PROTEIN SUBUNIT; SEA WATER;

ACTIVATION ENERGY; BACTERIUM; CHEMICAL COMPOUND; COLD TOLERANCE; ENZYME ACTIVITY; HOMOGENEITY; INHIBITION; PH; SEAWATER;

ANTARCTICA; ARTICLE; BACILLUS; CATALYSIS; COLD ACCLIMATIZATION; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME INHIBITION; ENZYME ISOLATION; ENZYME PURIFICATION; LOW TEMPERATURE; MESOPHILIC BACTERIUM; MOLECULAR WEIGHT; NONHUMAN; NUCLEOTIDE SEQUENCE; PH; PRIORITY JOURNAL; PSYCHROPHILIC BACTERIUM; SCAVENGING SYSTEM; THERMOSTABILITY;

ANTARCTIC REGIONS; BACILLUS; BACTERIAL PROTEINS; CATALASE; COLD TEMPERATURE; ENZYME STABILITY; KINETICS; MOLECULAR WEIGHT; SEAWATER;

BACILLUS (BACTERIUM); BACILLUS SP.; BACTERIA (MICROORGANISMS);

EID: 54249092929     PISSN: 00084166     EISSN: None     Source Type: Journal    
DOI: 10.1139/W08-066     Document Type: Article

References (27)

1. Ardissone, S., Frendo, P., Laurenti, E., Jantschko, W., Obinger, C., Puppo, A., and Ferrari, R.P. 2004. Purification and physical-chemical characterization of the three hydroperoxidases from the symbiotic bacterium Sinorhizobium meliloti. Biochemistry, 43: 12692-12699. doi:10.1021/bi048836s. PMID:15449959.
2. Beers, R.F., Jr., and Sizer, I.W. 1952. A spectrophotometric method for measuring the break down of hydrogen peroxide by catalase. J. Biol. Chem. 195: 276-287. PMID:14938361.
3. 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: 248-254. doi:10.1016/0003-2697(76)90527-3. PMID:942051.
4. Brown-Peterson, N.J., and Salin, M.L. 1995. Purification and characterization of a mesohalic catalase from the halophilic bacterium Halobacterium halobium. J. Bacteriol. 177: 378-384. PMID:7814327.
5. Cavicchioli, R., Siddiqui, K.S., Andrews, D., and Sowers, K.R. 2002. Low-temperature extremophiles and their applications. Curr. Opin. Biotechnol. 13: 253-261. doi:10.1016/S0958-1669(02)00317-8. PMID:12180102.
6. Chauvatcharin, N., Vattanaviboon, P., Switala, J., Loewen, P.C., and Mongkolsuk, S. 2003. Cloning and characterization of katA, encoding the major monofunctional catalase from Xanthomonas campestris pv. phaseoli and characterization of the encoded catalase KatA. Curr. Microbiol. 46: 83-87. doi:10.1007/s00284-002-3812-8. PMID:12520360.
7. Chelikani, P., Fita, I., and Loewen, P.C. 2004. Diversity of structures and properties among catalases. Cell. Mol. Life Sci. 61: 192-208. doi:10.1007/s00018-003-3206-5. PMID:14745498.
8. D'Amico, S., Marx, J.C., Gerday, C., and Feller, G. 2003. Activity stability relationships in extremophilic enzymes. J. Biol. Chem. 278: 7891-7896. doi:10.1074/jbc.M212508200. PMID:12511577.
9. Egidius, E., Wiik, R., Andersen, K., Hoff, K.A., and Hjeltnes, B. 1986. Vibrio salmonicida sp. nov., a new fish pathogen. Int. J. Syst. Bacteriol. 36: 518-520.
10. Feller, G., and Gerday, C. 2003. Psychrophilic enzymes: hot topics in cold adaptation. Nat. Rev. Microbiol. 1: 200-208. doi:10.1038/nrmicro773. PMID:15035024.
11. Fusho, Y., and Yajima, Y. 1996. Catalase from Bacillus subtilis IAM 1026 (Ferm BP-4844). US Patent 5486467. Available from www.patentstorm.us/ patents/5486467.html [accessed 7 August 2008].
12. Georlette, D., Blaise, V., Collins, T., D'Amico, S., Gratia, E., Hoyoux, A., et al. 2004. Some like it cold: biocatalysis at low temperatures. FEMS Microbiol. Rev. 28: 25-42. doi:10.1016/j.femsre.2003.07.003. PMID:14975528.
13. Hicks, D.B. 1995. Purification of three catalase isozymes from facultatively alkaliphilic from Bacillus firmus OF4. Biochim. Biophys. Acta, 1229: 347-355. doi:10.1016/0005-2728(95)00016-C. PMID:7748885.
14. Hoyoux, A., Blaise, V., Collins, T., D'Amico, S., Gratia, E., Huston, A.L., et al. 2004. Extreme catalysts from low-temperature environments. J. Biosci. Bioeng. 98: 317-330. doi:10.1016/S1389-1723(04)00290-7. PMID:16233714.
15. Klassen, G.R., Loewen, P.C., and Klotz, M.G. 1997. Phylogenetic relationships among prokaryotic and eukaryotic catalases. Mol. Biol. Evol. 14: 951-958. PMID:9287428.
16. Klotz, M.G., and Loewen, P.C. 2003. The molecular evolution of catalatic hydroperoxidases: evidence for multiple lateral transfer of genes between prokaryota and from bacteria into eukaryota. Mol. Biol. Evol. 20: 1098-1112. doi:10.1093/molbev/msg129. PMID:12777528.
17. Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond.), 227: 680-685. doi:10.1038/227680a0. PMID:5432063.
18. Lonhienne, T., Gerday, C., and Feller, G. 2000. Psychrophilic enzymes: revisiting the thermodynamic parameters of activation may explain local flexibility. Biochim. Biophys. Acta, 1543: 1-10. doi:10.1016/S0167- 4838(00)00210-7. PMID:11087936.
19. Lorentzen, M.S., Moe, E., Jouve, H.M., and Willassen, N.P. 2006. Cold adapted features of Vibrio salmonicida catalase: characterisation and comparison to the mesophilic counterpart from Proteus mirabilis. Extremophiles, 10: 427-440. doi:10.1007/s00792-006-0518-z. PMID:16609813.
20. Ni, J., Tokuyama, S., Sogabe, A., Kawamura, Y., and Tahara, Y. 2001. Cloning and high expression of catalase gene from Bacillus sp. TE124. J. Biosci. Bioeng. 91: 422-424. doi:10.1263/jbb.91.422. PMID:16233016.
21. Seaver, L.C., and Imlay, J.A. 2001. Hydrogen peroxide fluxes and compartmentalization inside growing Escherichia coli. J. Bacteriol. 183: 7182-7189. doi:10.1128/JB.183.24.7182-7189.2001. PMID:11717277.
22. Siddiqui, K.S., and Cavicchioli, R. 2006. Cold-adapted enzymes. Annu. Rev. Biochem. 75: 403-433. doi:10.1146/annurev.biochem.75.103004.142723. PMID:16756497.
23. Switala, J., and Loewen, P.C. 2002. Diversity of properties among catalases. Arch. Biochem. Biophys. 401: 145-154. doi:10.1016/S0003- 9861(02)00049-8. PMID:12054464.
24. Thompson, V.S., Schaller, K.D., and Apel, W.A. 2003. Purification and characterization of a novel thermo-alkali-stable catalase from Thermus brockianus. Biotechnol. Prog. 19: 1292-1299. doi:10.1021/bp034040t. PMID:12892493.
25. Woodbury, W., Spencer, A.K., and Stahman, M.A. 1971. An improved procedure using ferricyanide for detecting catalase isozymes. Anal. Biochem. 44: 301-305. doi:10.1016/0003-2697(71)90375-7. PMID:4109029.
26. Yumoto, I., Ichihashi, D., Iwata, H., Istokovics, A., Ichise, N., Matsuyama, H., et al. 2000. Purification and characterization of a catalase from the facultatively psychrophilic bacterium Vibrio rumoiensis S-1T exhibiting high catalase activity. J. Bacteriol. 182: 1903-1909. doi:10.1128/JB.182.7.1903-1909.2000. PMID:10714995.
27. Zámocký, M., Godočíková, J., Gašperík, J., Koller, F., and Polek, B. 2004. Expression, purification, and sequence analysis of catalase-1 from the soil bacterium Comamonas terrigena N3H. Protein Expr. Purif. 36: 115-123. doi:10.1016/j.pep.2004.03.001. PMID:15177292.