Articles & Issues
- Language
- english
- Conflict of Interest
- In relation to this article, we declare that there is no conflict of interest.
- Publication history
-
Received September 21, 2016
Accepted October 25, 2016
-
This is an Open-Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/bync/3.0) which permits
unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
Copyright © KIChE. All rights reserved.
All issues
L-DOPA Synthesis Using Tyrosinase-immobilized on Electrode Surfaces
Interdisciplinary Program of Graduate School for Bioenergy and Biomaterials, Chonnam National University, 77, Yongbong-ro, Buk-gu, Gwangju, 61186, Korea 1Department of Bioscience and Technology, Karunya University, Coimbatore, 641114, India 2Bioprocess Engineering Research Group, Chemical Engineering Department, Faculty of Engineering, Universitas Indonesia, Kampus UI Depok, 16424, Indonesia 3Department of Biotechnology and Bioengineering, Pukyong National University, 45, Yongso-ro, Nam-gu, Busan, 48513, Korea 4Department of Biotechnology and Bioengineering, Chonnam National University, 77, Yongbong-ro, Buk-gu, Gwangju, 61186, Korea
dhpark@chonnam.ac.kr
Korean Chemical Engineering Research, December 2016, 54(6), 817-821(5), 10.9713/kcer.2016.54.6.817 Epub 5 December 2016
Download PDF
Abstract
Levodopa or L-3,4-dihydroxyphenylalanine (L-DOPA) is the direct precursor of the neurotransmitter dopamine. L-DOPA is a well-known neuroprotective agent for the treatment of Parkinson’s disease symptoms. L-DOPA was synthesized using the enzyme, tyrosinase, as a biocatalyst for the conversion of L-tyrosine to L-DOPA and an electrochemical method for reducing L-DOPAquinone, the product resulting from enzymatic synthesis, to L-DOPA. In this study, three electrode systems were used: A glassy carbon electrode (GCE) as working electrode, a platinum, and a Ag/AgCl electrode as auxiliary and reference electrodes, respectively. GCE has been modified using electropolymerization of pyrrole to facilitate the electron transfer process and immobilize tyrosinase. Optimum conditions for the electropolymerization modified electrode were a temperature of 30 °C and a pH of 7 producing L-DOPA concentration 0.315 mM. After 40 days, the relative activity of an enzyme for electropolymerization remained 38.6%, respectively.
References
Blaser HU, Schmidt E, (Eds.), Asymmetric Catalysis on Industrial Scale: Challenges, Approaches, and Solutions, Wiley-VCH Verlag GmbH & Co, Weinheim (2004).
Knowles WS, Sabacky MJ, Vineyad, L-DOPA process and intermediates, United States Patent. US4005127 (1977).
Koyanagi T, Katayama T, Suzuki H, Nakazawa H, Yokozeki K, Kumagai H, J. Biotechnol., 115, 303 (2005)
Sayyed IA, Sudalai A, Tetrahedron: Asymmetry, 15, 3111 (2004)
Park HS, Lee JY, Kim HS, Biotechnol. Bioeng., 58(2-3), 339 (1998)
Kyanagi T, Katayama T, Suzuki H, Nakazawa H, Yokozeki K, Kumagai H, J. Biotechnol., 115, 303 (2005)
Huang SY, Shen YW, Chan HS, Enzyme Microb. Technol., 30(6), 779 (2002)
Krishnaveni R, Rathod V, Nagur R, Kulkarni P, Desai P, Int. J. Curr. Microbiol. App. Sci., 4(10), 350 (2015)
Wei T, Cheng BY, Liu JZ, Sci. Rep., 6, 30080 (2016)
Min K, Park K, Park DH, Yoo YJ, Appl. Microbiol. Biotechnol., 99(2), 575 (2015)
Zaborsky, Oskar, Immoblized Enzymes, CRC Press, Ohio (1974).
Guisan JM, Immobilization of Enzyme and Cells, Human Press, Totowa (2006).
Rahman SF, Min K, Park SH, Park JH, Yoo JC, Park DH, Korean J. Chem. Eng., 10.1007/s11814-016-0207-2 (2016)
Yildiz HB, Caliskan S, Kamaci M, Caliskan A, Int. J. Biol. Macromol., 56, 34 (2013)
Min K, Park DH, Yoo YJ, J. Biotechnol., 146, 40 (2010)
Rahman SF, Gobikishnan S, Indrawan N, Park SH, Park JH, Min K, Yoo YJ, Park DH, J. Microbiol. Biotechnol., 22, 1446 (2012)
Venugopal N, Kim WS, Korean J. Chem. Eng., 32(9), 1918 (2015)
Sadki S, Schottland P, Brodie N, Sabouraud G, Chem. Soc. Rev., 29, 283 (2000)
Liu X, Zhang Z, Cheng G, Dong S, Electroanalysis, 15, 2 (2003)
Ramanavicius A, Ramanaviciene A, Malinauskas A, Electrochim. Acta, 27, 6025 (2006)
Erdogan H, Tuncagil S, Toppare L, J. Macromol. Sci. A, 47, 209 (2010)
Kumar A, Gross RA, Biomacromolecules, 1(1), 133 (2000)
Cao X, Zhang R, Tan WM, Wei C, Wang J, Liu ZM, Chen KQ, Quyang PK, Korean J. Chem. Eng., 33(5), 1653 (2016)
Knowles WS, Sabacky MJ, Vineyad, L-DOPA process and intermediates, United States Patent. US4005127 (1977).
Koyanagi T, Katayama T, Suzuki H, Nakazawa H, Yokozeki K, Kumagai H, J. Biotechnol., 115, 303 (2005)
Sayyed IA, Sudalai A, Tetrahedron: Asymmetry, 15, 3111 (2004)
Park HS, Lee JY, Kim HS, Biotechnol. Bioeng., 58(2-3), 339 (1998)
Kyanagi T, Katayama T, Suzuki H, Nakazawa H, Yokozeki K, Kumagai H, J. Biotechnol., 115, 303 (2005)
Huang SY, Shen YW, Chan HS, Enzyme Microb. Technol., 30(6), 779 (2002)
Krishnaveni R, Rathod V, Nagur R, Kulkarni P, Desai P, Int. J. Curr. Microbiol. App. Sci., 4(10), 350 (2015)
Wei T, Cheng BY, Liu JZ, Sci. Rep., 6, 30080 (2016)
Min K, Park K, Park DH, Yoo YJ, Appl. Microbiol. Biotechnol., 99(2), 575 (2015)
Zaborsky, Oskar, Immoblized Enzymes, CRC Press, Ohio (1974).
Guisan JM, Immobilization of Enzyme and Cells, Human Press, Totowa (2006).
Rahman SF, Min K, Park SH, Park JH, Yoo JC, Park DH, Korean J. Chem. Eng., 10.1007/s11814-016-0207-2 (2016)
Yildiz HB, Caliskan S, Kamaci M, Caliskan A, Int. J. Biol. Macromol., 56, 34 (2013)
Min K, Park DH, Yoo YJ, J. Biotechnol., 146, 40 (2010)
Rahman SF, Gobikishnan S, Indrawan N, Park SH, Park JH, Min K, Yoo YJ, Park DH, J. Microbiol. Biotechnol., 22, 1446 (2012)
Venugopal N, Kim WS, Korean J. Chem. Eng., 32(9), 1918 (2015)
Sadki S, Schottland P, Brodie N, Sabouraud G, Chem. Soc. Rev., 29, 283 (2000)
Liu X, Zhang Z, Cheng G, Dong S, Electroanalysis, 15, 2 (2003)
Ramanavicius A, Ramanaviciene A, Malinauskas A, Electrochim. Acta, 27, 6025 (2006)
Erdogan H, Tuncagil S, Toppare L, J. Macromol. Sci. A, 47, 209 (2010)
Kumar A, Gross RA, Biomacromolecules, 1(1), 133 (2000)
Cao X, Zhang R, Tan WM, Wei C, Wang J, Liu ZM, Chen KQ, Quyang PK, Korean J. Chem. Eng., 33(5), 1653 (2016)
