Abstract
Lipase from Serratia marcescens VT 1 with a molecular weight of 62 kDa was purified by 9.42 fold with 16.89 % recovery by DEAE Cellulose and Sephadex G-75 columns. The characterization studies showed the optimum temperature and pH were 30 °C and 7, with good stability from 10 to 30 °C and pH 7. The lipase displayed good stability in the presence of metal ions Ca2+ and Na+, surfactants Gum arabic and Triton X-100, inhibitor EDTA, and organic solvents hexane and methanol. The serine inhibitor PMSF reduced lipase activity by 66 %. Vmax and Km kinetic parameters were 35.21 μmol/ml/min and 0.823 mM with p-nitrophenyl palmitate as substrate. The induction of methyl palmitate, methyl stearate, methyl oleate, and methyl linoleate from palm oil was confirmed by fatty acid methyl ester (FAME) analysis. The present study showed that the Serratia marcescens VT 1 lipase is a psychrophilic, neutral, and serine lipase efficacious of methyl esters genesis.
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