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Abstract

PHARMACEUTICALLY SIGNIFICANT ENZYMES- TYROSINASE AND ASPERGINASE FROM MESOPHILIC STREPTOMYCES-A3DR2S

Dr. D. R. Majumder*, Sara Lambate, Aqsa Firfire, Rahat Palekar, Asfiya Shaikh, Ashlesha Bhandari and Reshma Sayyed

Abstract

In the present study, Actinomycete strain producing Tyrosinase, Asparginase, along with Amylase, Protease and Lipase was isolated from garden soil. Tyrosinase and Asparginase were chosen for further study because of their pharmaceutical and commercial importance. Tyrosinase catalyzes the bioconversion of an amino acid L-Tyrosine to L-DOPA (3,4dihydroxyphenylalanine). L-DOPA has therapeutic importance in the treatment of Parkinson’s disease. L-asparginase also known as L-asparagine amidohydrolase, is the enzyme with anti-tumor activity and used as a chemotherapeutic agent against acute lymphoblastic leukemia and lymphosarcoma. From microscopic observation the isolate was identified as Streptomyce sp A3DR2S. The optimization result revealed that the maximum Tyrosinase and L-DOPA production was at pH-8 and room temperature 370C with ideal substrate concentration of 0.1%. Similarly, maximum production of Asparginase was recorded at pH 6.5 and temperature 370C with substrate concentration of 1%. Specific activity of tyrosinase was calculated to be 232.75U/mg and that of asparginase it was 4.30 U/mg. Purity of both the enzymes was checked by SDS-PAGE revealing the presence of a single band with a molecular weight of 38kDa for Tyrosinase and 150kDa for Asparginase approximately. Km and Vm of tyrosinase was calculated as 2.7mM and 5.4mM/ml/min and that of asparginase the values are 3.75mM and 7.5mM/ml/min.

Keywords: Streptomyce sp A3DR2S, Amylase, Protease, Lipase, Tyrosinase, Asparginase, L-DOPA.


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