Research Article | Volume: 8, Issue: 9, September, 2018

Isolation, Identification and Medium Optimization for Tyrosinase Production by a Newly Isolated Bacillus subtilis NA2 Strain

Elsayed Ahmed Elsayed ,  Enas Nabil Danial   
Elsayed Ahmed Elsayed1 & 3, Enas Nabil Danial2 & 3

1Bioproducts Research Chair, Zoology Department, Faculty of Science, King Saud University, 11451 Riyadh, Kingdom of Saudi Arabia.

2Applied Biochemistry Department, Faculty of Science, University of Jeddah, Jeddah, Saudi Arabia.

3Chemistry of Natural and Microbial Products Department, National Research Centre, Dokki, Cairo, Egypt.

Open Access   

Published:  Sep 30, 2018

DOI: 10.7324/JAPS.2018.8914
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Abstract

Tyrosinase (EC 1.14.18.1, monophenol, O-diphenol: oxygen oxidoreductase) is a copper-metallo-bifunctional enzyme, which catalyzes the O-hydroxylation and oxidation of monophenols to quinones. Tyrosinase plays an important role in the immune defense mechanisms of many prokaryotic and eukaryotic organisms. It also finds many applications in antioxidants and therapeutic fields. In the present work, a newly isolated tyrosinase-producing strain (Bacillus subtilis NA2) was identified using 16S rDNA and BLAST analysis. The primary cultivation medium produced tyrosinase at 416.67 U/min/mL with a yield coefficient (YP/X) of 111.75 × 103 U/g cells. Furthermore, the cultivation medium for the production of tyrosinase was optimized. The final optimized cultivation medium composed of (g/L): sucrose, 10; KNO3, 10; K2HPO4, 0.5; MgSO4.7H2O, 0.25; tyrosine, 10 and the initial optimized pH of the cultivation medium was 8.5. It has been shown, that the final optimized medium with the optimized pH resulted in an increase of about 39% in tyrosinase production from the initial un-optimized conditions. The new tyrosinase producing strain was identified and its volumetric production was significantly increased after the successful optimization of the production medium.


Keyword:     Isolation Identification Bacillus Tyrosinase Production Yield coefficient.

Citation:

Elsayed EA, Danial EN. Isolation, Identification and Medium Optimization for Tyrosinase Production by a Newly Isolated Bacillus subtilis NA2 Strain. J App Pharm Sci, 2018; 8(09): 093- 101.

Copyright: © The Author(s). This is an open-access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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Reference

Allouche N, Damak A, Ellouz R, Sayadi S. Use of whole cells of Pseudomonas aeruginosa for synthesis of the antioxidant hydroxytyrosol via conversion of tyrosol. Appl Environ Microbiol, 2004; 70(4):2105-2109. https://doi.org/10.1128/AEM.70.4.2105-2109.2004

Caf Y, MaaÅŸoÄŸlu Y, Valipour E, Arikan B. Production and characterization of novel cold-active, pH tolerant and detergent-stable: α-amylase from a psychrotrophic bacterium from soil samples. New Biotechnol, 2012; 29:S82. https://doi.org/10.1016/j.nbt.2012.08.227

Chaskes S, Cammer M, Nieves E, Casadevall A. Pigment production on L-tryptophan Medium by Cryptococcus gattii and Cryptococcus neoformans. PLoS One, 2014; 9(4):e91091. https://doi.org/10.1371/journal.pone.0091901

Claus H, Decker H. Bacterial tyrosinases. Syst Appl Microbiol, 2006; 29(1):3-14. https://doi.org/10.1016/j.syapm.2005.07.012

Dalfard AB, Khajeh K, Soudi MR, Naderi-Manesh H, Ranjbar B and Sajedi RH. Isolation and biochemical characterization of laccase and tyrosinase activities in a novel melanogenic soil bacterium. Enzyme Microb Technol, 2006; 39(7):1409-1416. https://doi.org/10.1016/j.enzmictec.2006.03.029

Danial NE, Al-Bishri WM. Optimization of medium composition for increased production of tyrosinase enzyme in recombinant Bacillus megaterium. Res J Pharm Biol Chem Sci, 2018; 9(1):480-486.

Decker H, Tuczek F. Tyrosinase/catecholoxidase activity of hemocyanins: structural basis and molecular mechanism. Trends Biochem Sci, 2000; 25(8):392-397. https://doi.org/10.1016/S0968-0004(00)01602-9

Edwards U, Rogall T, Blocker H, Emde M, Bottger EC. Isolation and direct complete nucleotide determination of entire genes. Nucleic Acids Res, 1989; 17:7843-7853. https://doi.org/10.1093/nar/17.19.7843

El-Enshasy HA, Elsayed EA. Kinetics of cell growth and invertase production by the biotherapeutic yeast, Saccharomyces boulardii. J Sci Ind Res, 2017; 76(8):477-484.

Franciscon E, Grossman MJ, Paschoal JA, Reyes FG, Durrant LR. Decolorization and biodegradation of reactive sulfonated azo dyes by a newly isolated Brevibacterium sp. strain VN-15. Springer Plus, 2012; 1(1):37. https://doi.org/10.1186/2193-1801-1-37

Herwig C, Doerries C, Marison I, Stockar U, Quantitative analysis of the regulation scheme of invertase expression in Saccharomyces cerevisiae. Biotechnol Bioeng, 2001; 76:247-258. https://doi.org/10.1002/bit.10004

Hullo MF, Moszer I, Danchin A, Martin-Verstraete I. CotA of Bacillus subtilis is a copper-dependent laccase. J Bacteriol, 2001; 183:5426- 5430. https://doi.org/10.1128/JB.183.18.5426-5430.2001

Ingle SS, Khobragade CN, Production and purification of the tyrosinase enzyme from soil bacteria. Helix, 2013; 6:436-440.

Kumar CG, Mongolla P, Pombala S, Kamle A, Joseph J. Physicochemical characterization and antioxidant activity of melanin from a novel strain of Aspergillus bridgeri ICTF-201. Lett Appl Microbiol, 2011; 53 (3):350-358. https://doi.org/10.1111/j.1472-765X.2011.03116.x

Lowry OH, Rosebrough NJ, Farr AL, Randal RJ. Protein measurement with the Folin phenol reagent. J Biol Chem, 1951; 193:265- 275.

Marino SM, Fogal S, Bisaglia M, Moro S, Scartabelli G, De Gioia L, Spada A, Monzani E, Casella L, Mammi S, Bubacco L. Investigation of Streptomyces antibioticus tyrosinase reactivity toward chlorophenols. Arch Biochem Biophys, 2011; 505(1):67-67. https://doi.org/10.1016/j.abb.2010.09.019

Pandey G, Muralikrishna C, Bhalerao UT. Mushroom tyrosinase catalyzed synthesis of coumestans, benzofuran derivatives and related heterocyclic-compounds. Tetrahedron, 1989; 45(21):6867-6874. https://doi.org/10.1016/S0040-4020(01)89154-7

Rao SKRS, Tripathy NK, Mahalaxmi Y, Prakasham RS. Laccase- and peroxidase-free tyrosinase production by isolated microbial strain. J Microbiol Biotchnol, 2012; 22(2):207-214. https://doi.org/10.4014/jmb.1106.06031

Rao SKRS, Tripathy NK, Rao SD, Prakasham RS. Production, characterization, catalytic and inhibitory activities of tyrosinase. Res J Biotechnol, 2013; 8(1):87-99.

Sambrook J, Fritsch EF, Maniatis T. Molecular cloning A. Laboratory Manual. Cold Spring Harbor Laboratory, NY. 1989.

Saratale RG, Saratale GD, Chang JS, Govindwar SP. Bacterials decolorization and degradation of azo dyes: A review. J Taiwan Inst Chem Eng, 2011; 42(1):138-157. https://doi.org/10.1016/j.jtice.2010.06.006

Sharma AD, Kainth S, Gill PK. Inulinase production using garlic (Allium sativum) powder as a potential substrate in Streptomyces sp. J Food Eng, 2006; 77:486-491. https://doi.org/10.1016/j.jfoodeng.2005.06.072

Seo SY, Sharma VK, Sharma N. Mushroom tyrosinase: Recent prospects. J Agric Food Chem, 2003; 51(10):2837-2853. https://doi.org/10.1021/jf020826f

Shuster V, Fishman A. Isolation, cloning and characterization of a tyrosinase with improved activity in organic solvents from Bacillus megaterium. J Mol Microbiol Biotechnol, 2009; 17(4):188-200. https://doi.org/10.1159/000233506

Surwase SN, Patil SA, Apine OA, Jadhav JP. Efficient microbial conversion of L-tyrosine to L-DOPA by Brevundimonas sp. SGJ. Appl Biochem Biotechnol, 2012b; 167:1015-1028. https://doi.org/10.1007/s12010-012-9564-4

Surwase SN, Patil SA, Jadhav SB, Jadhav JP. Optimization of l‐DOPA production by Brevundimonas sp. SGJ using response surface methodology. Microb Biotechnol, 2012a; 5(6):731-737. https://doi.org/10.1111/j.1751-7915.2012.00363.x

Valipour E, Arikan B. Optimization of tyrosinase enzyme production from native Bacillus sp. MV29 isolate. J Appl Biol Sci, 2015; 9(2):77-82.

Valipour E, Arikan B. Increased production of tyrosinase from Bacillus megaterium strain M36 by the response surface methods. Arch Biol Sci, 2016; 68(3):659-668. https://doi.org/10.2298/ABS151002058V

Xu DY, Chen JY, Yang Z. Use of cross-linked tyrosinase aggregates as catalyst for synthesis of L-DOPA. Biochem Eng J, 2012; 63:88-94. https://doi.org/10.1016/j.bej.2011.11.009

Zhang T, Wen S, Tan T. Optimization of the medium for glutathione production in Saccharomyces cerevisiae. Process Biochem, 2007; 42:454-458. https://doi.org/10.1016/j.procbio.2006.09.003

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