International E-publication: Publish Projects, Dissertation, Theses, Books, Souvenir, Conference Proceeding with ISBN.  International E-Bulletin: Information/News regarding: Academics and Research

Isolation, purification and characterization of tyrosinase from Allium sativum

    , , ,

Author Affiliations

  • 1Department of PG studies in Biotechnology, Government Science College (Autonomous), Bengaluru, Karnataka, India
  • 2Department of PG studies in Biotechnology, Government Science College (Autonomous), Bengaluru, Karnataka, India
  • 3Department of PG studies in Biotechnology, Government Science College (Autonomous), Bengaluru, Karnataka, India
  • 4Department of PG studies in Biotechnology, Government Science College (Autonomous), Bengaluru, Karnataka, India

Int. Res. J. Biological Sci., Volume 10, Issue (2), Pages 8-15, May,10 (2021)

Abstract

Alzheimer\'s and Parkinson\'s are neurological disorders. Alzheimer\'s is a progressive neurodegenerative disorder that destroys memory with important mental functions. Parkinson\'s affects the central nervous system, it impairs movement, often including tremors for which there is no cure. Currently dopamine, a neurotransmitter is used in the treatment of these disorders. Tyrosinase (E.C 1.14.18.1) is an enzyme that catalyzes L- Tyrosine into L- DOPA a precursor for the synthesis of dopamine. Tyrosinase is present in sources like fungi, plants, animals. Very few work on tyrosinase has been reported in plants. In our present investigation tyrosinase was isolated and purified from Allium sativum (Garlic ) and enzyme activity was carried out using UV - visible spectroscopy and the enzymatic activity was found to be 180 U/ ml. The kinetic parameters were studied and the optimum temperature was found to be 30ºC and the optimum pH was found to be pH 7. Saturation with increasing substrate concentration was found to be at 1200 U/ml. The enzyme was subjected to a series of purification steps that includes ammonium sulphate precipitation, dialysis, ion-exchange chromatography, and gel filtration chromatography. The maximum purification fold of the enzyme was found to be 97.58. SDS - PAGE was performed to determine the molecular weight and was reported to be 98 KDa. Hence through this research work, we have tried to identify a novel source of tyrosinase in Allium sativum.

References

  1. Kanteev, M., Goldfeder, M., & Fishman, A. (2015). Structure-function correlations in tyrosinases. Protein Science, 24(9), 1360-1369., undefined, undefined
  2. Kumar CM, Sathisha UV, Dharmesh S, Rao AG, Singh SA (2011). Interaction of sesamol (3,4-methylenedioxy phenol) with tyrosinase and its effect on melanin synthesis. Biochimie, 93(3), 562-9., undefined, undefined
  3. Xu, J. J., Fang, X., Li, C. Y., Yang, L., & Chen, X. Y. (2020). General and specialized tyrosine metabolism pathways in plants. A Biotech, 1(2), 97-105., undefined, undefined
  4. Mitchell, R. A., Herrmann, N., & Lanctôt, K. L. (2011). The role of dopamine in symptoms and treatment of apathy in Alzheimer, undefined, undefined
  5. Bonuccelli, U., & Pavese, N. (2006). Dopamine agonists in the treatment of Parkinson’s disease. Expert Review of Neurotherapeutics, 6(1), 81-89. https://doi.org/10.1586/14737175.6.1.81, undefined, undefined
  6. Armando, I., Villar, V. A. M., & Jose, P. A. (2011). Dopamine and Renal Function and Blood Pressure Regulation. Comprehensive Physiology 1(3), 1075-1117. https://doi.org/10.1002/cphy.c100032, undefined, undefined
  7. Martorana, A., Stefani, A., Palmieri, M. G., Esposito, Z., Bernardi, G., Sancesario, G., & Pierantozzi, M. (2008). l-dopa modulates motor cortex excitability in Alzheimer’s disease patients. Journal of Neural Transmission, 115(9), 1313-1319., undefined, undefined
  8. Dorszewska, J., Prendecki, M., Lianeri, M., & Kozubski, W. (2014). Molecular Effects of L-dopa Therapy in Parkinson’s Disease. Current Genomics, 15(1), 11-17., undefined, undefined
  9. Zolghadri, S., Bahrami, A., Hassan Khan, M. T., Munoz-Munoz, J., Garcia-Molina, F., Garcia-Canovas, F., & Saboury, A. A. (2019). A comprehensive review on tyrosinase inhibitors. Journal of Enzyme Inhibition and Medicinal Chemistry, 34(1), 279-309., undefined, undefined
  10. Selvarajan, E., Veena, R., & Kumar, N. M. (2018). Polyphenol oxidase, beyond enzyme browning. In Microbial bioprospecting for sustainable development (pp. 203-222). Springer, Singapore., undefined, undefined
  11. Selinheimo, E., Lampila, P., Mattinen, M.-L., & Buchert, J. (2008). Formation of Protein−Oligosaccharide Conjugates by Laccase and Tyrosinase. Journal of Agricultural and Food Chemistry, 56(9), 3118-3128., undefined, undefined
  12. Lantto, R., Plathin, P., Niemistö, M., Buchert, J., & Autio, K. (2006). Effects of transglutaminase, tyrosinase, and freeze-dried apple pomace powder on gel-forming and structure of pork meat. LWT - Food Science and Technology, 39(10), 1117-1124., undefined, undefined
  13. Selinheimo, E., Autio, K., Kruus, K., & Buchert, J. (2007). Elucidating the Mechanism of Laccase and Tyrosinase in Wheat Bread Making. Journal of Agricultural and Food Chemistry, 55(15), 6357-6365., undefined, undefined
  14. Svitel, J. (1998). Development of Tyrosinase-Based Biosensor and Its Application for Monitoring of Bioremediation of Phenol and Phenolic Compounds. Environmental Science & Technology, 32(6), 828-832., undefined, undefined
  15. Lowry OH, Rosebrough NJ, Farr AL and Randall RJ (1951). Protein measurement with the Folin phenol reagent. J Biol Chem. Nov; 193(1), 265-275., undefined, undefined
  16. Duckworth, H. W., & Coleman, J. E. (1970). Physicochemical and kinetic properties of mushroom tyrosinase. Journal of Biological Chemistry, 245(7), 1613-1625., undefined, undefined
  17. Stoscheck, C. M. (1990). Quantitation of protein [6]. Guide to Protein Purification, 50-68., undefined, undefined
  18. Ikram-ul-Haq, Ali, S., & Qadeer, M. A. (2002). Biosynthesis of L-DOPA by Aspergillusoryzae. Bioresource Technology, 85(1), 25-29., undefined, undefined