Natural overproduction of catalase by Kocuria sp. ASB 107: extraction and semi-purification
Abstract
Background and Objectives: Because of importance of catalase in various industries, efforts have been made to find more suitable bacterial sources for catalase production. Kocuria is one of well-known catalase-producing genus. This is the first report about a new catalase-overproducing bacterial strain, Kocuria sp. ASB 107.
Materials and Methods: Kocuria sp. ASB 107 had been isolated from Abe-Siah Spring in Ramsar in our previous report. The bacterial biomass freezed, thawed and then lysed by three different operations separately: ultrasound, lysing buffer and enzymatic digestion. The crude extract was subjected to ammonium sulfate precipitation (40 and 60% saturation). Quality and quantity of the semi-purification was checked by electrophoresis and measuring specific activity, respectively.
Results: Kocuria sp. ASB 107 can be lysed by a freeze-thaw stage followed by lysozyme digestion and not by lysing buffer and not by ultrasound. Surprisingly specific activity of catalase in crude extract from Kocuria sp. ASB 107 was measured to be 195, 370 U/mg protein which is too much higher than other bacterial strains. The bacterium showed a relatively long growth curve about 40 hours. Semi-purification using ammonium sulfate precipitation was led in an increased specific activity up to about 7×106 U/mg protein implying more than 3.6-fold purification.
Conclusion: We have showed natural catalase-overproducing ability of Kocuria sp. ASB 107. Yield and purity of catalase from Kocuria sp. ASB 107 showed great potential in industrial application suggesting the strain as good source for mass production of catalase for treatment of H2O2-containing wastewater in comparison to other bacterial sources.
Loew OA. New enzyme of general occurrence in organisms. Science 1900; 11(279): 701-702.
Dantas AS, Andrade RV, de Carvalho MJ, Felipe MSS, Campos EG. Oxidative stress response in Paracoccidioides brasiliensis: assessing catalase and cytochrome c peroxidase. Mycol Res 2008; 112(Pt 6): 747-756.
Schrader M, Fahimi HD. Peroxisomes and oxidative stress. Biochim Biophys Acta 2006; 1763: 1755-1766.
Watt BE, Proudfoot AT, Vale JA. Hydrogen peroxide poisoning. Toxicol Rev 2004; 23:51-57.
Tran L, Orth R, Parashos P, Tao Y, Tee CW, Thomas VT, et al. Depletion rate of hydrogen peroxide from sodium perborate bleaching agent. J Endod 2017; 43:472-476.
Ciriminna R, Albanese L, Meneguzzo F, Pagliaro M. Hydrogen peroxide: A Key chemical for today's sustainable development. ChemSusChem 2016; 9:3374-3381.
Hughes R, Kilvington S. Comparison of hydrogen peroxide contact lens disinfection systems and solutions against Acanthamoeba polyphaga. Antimicrob Agents Chemother 2001; 45: 2038-2043.
Doshi R, Shelk V. Enzyme in textile industry-An enviroment-friendly approach. IJFTR 2001; 26(1-2): 202-205.
Rochat T, Gratadoux JJ, Gruss A, Corthier G. Production of heterologous nonheme catalase by actobacillus casei: an efficient tool for removal of H2O2 and protection of Lactobacillus bulgaricus from oxidative stress in milk. Appl Environ Microbiol 2006; 72: 5143-5149.
Paar A, Costa S, Tzanov T, Gudelj M, Robra KH, Cavaco-Paulo A, et al. Thermo-alkali-stable catalases from newly isolated Bacillus sp. for the treatment and recycling of textile bleaching effluents. J Biotechnol 2001; 89(2-3): 147-149.
Zeng HW, Cai YJ, Liao XR, Zhang F, Zhang D. Production, characterization, cloning and sequence analysis of a monofunctional catalase from Serratia marcescens SYBC08. J Basic Microbiol 2011; 51: 205-214.
Fu X, Wang W, Hao J, Zhu X, Sun M. Purification and characterization of catalase from marine bacterium Acinetobacter sp. YS0810. Biomed Res Int 2014; 2014: 409626.
Susmitha S, Ranganayaki P, Vidyamol KK, Vijayaraghavan R. Purification and characterization of catalase enzyme from Agaricus bisporus. Int J Curr Microbiol 2013; 2(12): 255-263.
Yumoto I, Ichihashi D, Iwata H, Istokovics A, Ichise .N, Matsuyama I, et al. Purification and characterization of a catalase from the facultatively psychrophilic bacterium Vibrio rumoiensis S-1T exhibiting high catalase activity. J Bacteriol 2000; 182: 1903-1909.
Ali Hussein A. Purification and characterization of thermo-alkali stable catalase from Bacillus sp. Int Res J Biotechnol 2012; 3: 207-214.
Asgarani E, Soudi MR, Borzooee F, Dabbagh R. Radio-resistance in psychrotrophic Kocuria sp. ASB 107 isolated from Ab-e-Siah radioactive spring. J Environ Radioact 2012; 113: 171-176.
Rendón OZ, Neiva LS, Sasarman F, Shoubridge EA. The arginine methyltransferase NDUFAF7 is essential for complex I assembly and early vertebrate embryogenesis. Hum Mol Genet 2014; 23: 5159-5170.
Beers RF Jr, Sizer IW. A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J Biol Chem 1952; 195: 133-140.
Hadwan MH, Najm Abed H. Data supporting the spectrophotometric method for the estimation of catalase activity. Data Brief 2016; 6: 194-199.
Brown-Peterson NJ, Salin ML. Purification and characterization of a Mesohalic catalase from the halophilic bacterium Halobacterium halobium. J Bacteriol 1995; 177: 378-384.
Zeng HW, Cia YJ, Liao XR, Qian SL, Zhang F, Zhang DB. Optimization of catalase production and purification and characterization of a noval cold-adapted Cat-2 from mesophilic bacterium Serratia marcescens SYBC-01. Ann Microbiol 2010; 60: 701-708.
Bradford MM. Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976; 72: 248-254.
Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227(5259):680-685.
Shi X, Feng M, Zhao Y, Guo X, Zhou P. Overexpression, purification and characterization of a recombinant secretary catalase from Bacillus subtilis. Biotechnol Lett 2008; 30:181-186.
Loewen PC, Switala J. Purification and characterization of catalase-1 from Bacillus subtilis. Biochem Cell Biol 1987; 65: 939-947.
Gudelj M, Fruhwirth GO, Paar A, Lottspeich F, Robra KH, Cavaco-Paulo A, et al. A catalase-peroxidase from a newly isolated thermoalkaliphilic Bacillus sp. with potential for the treatment of textile bleaching effluents. Extremophiles 2001; 5: 423-429.
Mizobata T, Kagawa M, Murakoshi N, Kusaka E, Kameo K, Kawata Y, et al. Overproduction of thermus sp. YS 8-13 manganese catalase in Escherichia coli. production of soluble apoenzyme and in vitro formation of active holoenzyme. Eur J Biochem 2000; 267: 4264-4271.
Chagas RF, Bailao AM, Fernandes KF, Winters MS, Pereira M, Soares CMDA. Purification of Paracoccidioides brasiliensis catalase P: subsequent kinetic and stability studies. J Biochem 2010; 147: 345-351.
Johnsson K, Froland WA, Schultz PG. Overexpression, purification, and characterization of the catalase-peroxidase KatG from Mycobacterium tuberculosis. J Biol Chem 1997; 272: 2834-2840.
El-Sharouny EE, Belal MA, Yusef HH. Isolation and characterization of two novel local psychrotolerant Kocuria spp. with high affinity towards metal cations biosorption. Life Science J 2013; 10(4): 1721-1737.
Seo YB, Kim D, Kim G, Kim H, Nam S, Kim YT, et al. Kocuria gwangalliensis sp. nov., an actinobacterium isolated from seawater. Int J Syst Evol Microbiol 2009; 59(Pt 11):2769-2772.
Mehrabadi JF, Mirzaie A, Ahangar N, Rahimi A, Rokni-Zadeh H. Draft genome sequence of Kocuria rhizophila RF, a radiation-resistant soil isolate. Genome Announc 2016; 4(2): e00095-16.
Gholami M, Etemadifar Z, Bouzari M. Isolation a new strain of Kocuria rosea capable of tolerating extreme conditions. J Environ Radioact 2015; 144:113-119.
Loprasert S, Vattanaviboon P, Praituan W, Chamnongpol S, Mongkolsuk S. Regulation of the oxidative stress protective enzymes, catalase and superoxide dismutase in Xanthomonas-a review. Gene 1996; 179:33-37.
Yun EJ and Lee YN. Production of two different catalase-peroxidases by Deinococcus radiophilus. FEMS Microbiol Lett 2000; 184:155-159.
Jia X, Chen J, Lin C, Lin X. Cloning, expression, and characterization of a novel thermophilic monofunctional catalase from Geobacillus sp. CHB1. Biomed Res Int 2016; 2016: 7535604.
Nakayama M, Nakajima-Kambe T, Katayama H, Higuchi K, Kawasaki Y, Fuji R. High catalase production by Rhizobium radiobacter strain 2-1. J Biosci Bioeng 2008; 106: 554-558.
Hochman A, Shemesh A. Purification and characterization of a catalase-peroxidase from the photosynthetic bacterium Rhodopseudomonas capsulata. J Biolog Chem 1987; 262: 6871-6876.
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Issue | Vol 9 No 6 (2017) | |
Section | Original Article(s) | |
Keywords | ||
Kokuria Catalase Overproduction Extraction Semi-purification |
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