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Immobilization of alkaline protease from Conidiobolus macrosporus for reuse and improved thermal stability

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Abstract

Alkaline protease from Conidiobolus macrosporus was immobilized on polyamide using glutaraldehyde as a bifunctional agent. The immobilized enzyme was optimally active at a higher temperature of 50 °C than the free enzyme (40 °C ) and showed a ten-fold increased thermostability at 60 °C compared to that of the free enzyme. The efficiency of immobilization was 58% under the optimal conditions of pH and temperature. There was a 14-fold decrease in the K m of immobilized enzyme compared to the free enzyme. The immobilized enzyme was fully active even after twenty-two cycles of repeated use. It retained 80% activity at 50 °C in presence of 8 M urea exhibiting its stability to the denaturant and was compatible with several commercial detergents.

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Authors and Affiliations

  1. Division of Biochemical Sciences, National Chemical Laboratory, Pune, 411 008, India

    Aparna Tanksale, P. Manish Chandra, Mala Rao & Vasanti Deshpande

Authors
  1. Aparna Tanksale
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  2. P. Manish Chandra
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  3. Mala Rao
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  4. Vasanti Deshpande
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Tanksale, A., Chandra, P.M., Rao, M. et al. Immobilization of alkaline protease from Conidiobolus macrosporus for reuse and improved thermal stability. Biotechnology Letters 23, 51–54 (2001). https://doi.org/10.1023/A:1026782206945

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  • DOI: https://doi.org/10.1023/A:1026782206945

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