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  • 1 Department of Biotechnology, Himachal Pradesh University, Summer Hill Shimla-171 005, Indi
  • 2 Department of Biotechnology, Himachal Pradesh University, Summer Hill Shimla-171 005, Indi
  • 3 Department of Biotechnology, Himachal Pradesh University, Summer Hill Shimla-171 005, Indi
  • 4 Department of Chemistry, Guru Nanak Dev University Amritsar-143 005, India
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An alkaline thermotolerant lipase of Bacillus coagulans BTS1 was successively purified by ammonium sulfate precipitation and DEAE anion exchange chromatography. The purified lipase immobilized in alginate beads showed an optimal activity at pH 7.5 and 55ºC. A pH of 5.0 or 10.0 completely quenched the activity of immobilized lipase. The alginate-bound lipase retained its activity following exposure to most of the organic solvents including amines, alkanes and alcohols. Chloride salt of Al3+, Co2+, Mg2+ and NH4+ modulated the lipase activity of alginate-immobilized enzyme. The alginate entrapped lipase showed a preferentially high activity towards p-nitrophenyl palmitate (C: 16) and activity of matrix increased following exposure to SDS. Moreover, the immobilized lipase retained more than 50% of its activity after 3rd cycle of reuse.

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