Abstract
Microbial lipases are known for their industrial applications. Aspergillus eucalypticola was used for mutagenesis using Ethyl methanesulfonate. Mutagen-treated strain (MTS-03) of A. eucalypticola resulted in 119.05 ± 0.14 IU/ml/min lipase activity as compared to Lipolytic fungal strain (LFS-7) of A. eucalypticola which resulted in 88.98 ± 0.21 IU/ml/min. The purified enzyme resulted 51.03 fold increase for MTS-03 lipase and 23.06 fold increase for LFS-7 lipase. The MTS-03 lipase was found stable between 25 °C to 55 °C and alkaline pH 8 to pH 11. The residual activity of MTS-03 and LFS-7 lipase was increased to 124.42 % and 114.23 %, respectively in the presence of magnesium ion. The MTS-03 lipase was found to be highly stable in methanol solvent with 127.82 % residual activity and exhibited 111.16 % residual activity in presence of 15 % (v/v) Triton X-100 and stable in presence of Patanjali detergent with 120.14 % residual activity. The efficient stability of obtained lipase suggests its potential usage in industries.
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