Partial Purification and Biochemical Characterisation of a Novel Thermos Table Extracellular Lipase from Serratia Marcescens SCL1 Isolated from Medicinal Waste
Lipases find wide application in modern industrialization. Thermostable lipases are a challenge for various applications in different industrial segments. Microbial enzymes are a cheap source of lipase. In the present study isolation, partial purification and characterization of a novel thermostable lipase produced from Serratia marcescens scl1 was carried out. The lipase producing bacteria was isolated from medicinal waste and identified as Serratia marcescens using 16S rDNA sequencing method. Biochemical characterization performed showed the optimum growth conditions for the bacteria at 37°C temperature, pH7 in production media using 1% (w/v) olive oil as a carbon source, after 48 hours of incubation. Extracellular lipase produced by the bacteria was partially purified by ammonium sulphate precipitation and dialysis. Biochemical characterization revealed that the enzyme showed optimum activity at temperature 75°C and pH 8. The substrate saturation kinetics showed maximum at 1.3mM [S] and activity 5.43±0.05 X10-2 unit/ml. The protein concentration determined is 240µg/ml and specific activity of the enzyme is 22.58 unit/mg. The quantitative assay of lipase activity was carried out using 2.0 mM pNPP as substrate in 50.0mM Tris-HCl measuring absorbance at 410nm. The study revealed that isolated bacterium is able to produce a thermostable lipase which can satisfy the requirements of modern industrialization.