International Science Community Association International Research Journal of Biological Sciences 2278-3202 10 2 2021 05 10 Isolation, purification and characterization of tyrosinase from Allium sativum 8 15 EN Kumar S. Akhil 1 Department of Animal Science, Manonmaniam Sundaranar University, Tirunelveli, Tamil Nadu, India Muthulakshmi M. 2 Department of Animal Science, Manonmaniam Sundaranar University, Tirunelveli, Tamil Nadu, India Manju 3 Department of Animal Science, Manonmaniam Sundaranar University, Tirunelveli, Tamil Nadu, India Palavesam A. 4 L. Satish 1 Department of PG studies in Biotechnology, Government Science College (Autonomous), Bengaluru, Karnataka, India M. Nikhil 2 Department of PG studies in Biotechnology, Government Science College (Autonomous), Bengaluru, Karnataka, India L. Sandeep 3 Department of PG studies in Biotechnology, Government Science College (Autonomous), Bengaluru, Karnataka, India Khabade Sarina P. 4 Department of PG studies in Biotechnology, Government Science College (Autonomous), Bengaluru, Karnataka, India > Research Paper 2020 10 15 2021 05 10 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. Copyright@ International Science Community Association