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A novel thermostable lipase from a thermophilic Bacillus sp.: characterization and esterification studies

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Abstract

An extracellular, thermostable, alkaline lipase was partially purified from a thermophilic Bacillus strain J 33. It was optimally active at pH 8.0 at 60°C, retaining 50% activity at 70°C for 30 min. It had native molecular mass of 45 kDa. The lipase was stable in 90% (v/v) hexane or benzene mixtures in water. It converted 66% oleic acid at 0.25 M with 0.4 M methanol in hexane to methyl oleate at 60°C in 16 h. Activity was stimulated by Mg2 (10 mM) but inhibited by EDTA (10 mM) and PMSF (10 mM). It was stable in Triton X-100, Tween 20 and Tween 80 (0.1% v/v). © Rapid Science Ltd. 1998

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Authors and Affiliations

  1. Department of Biotechnology, Panjab University, Chandigarh, India

    Nirupama Nawani, Nirpjit S. Dosanjh & Jagdeep Kaur

Authors
  1. Nirupama Nawani
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  2. Nirpjit S. Dosanjh
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  3. Jagdeep Kaur
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Nawani, N., Dosanjh, N.S. & Kaur, J. A novel thermostable lipase from a thermophilic Bacillus sp.: characterization and esterification studies. Biotechnology Letters 20, 997–1000 (1998). https://doi.org/10.1023/A:1005414428737

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  • DOI: https://doi.org/10.1023/A:1005414428737

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