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Single-step purification and immobilization of penicillin acylase using hydrophobic ligands

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Abstract

Five differenthydrophobic ligands immobilized on 4% (4XL) and 6% (6XL) crosslinked agarose were used to study the single-step purification of penicillin acylase from cell lysate. The 4XL gels showed relatively higher specific activity and recovery than the 6XL gels. In single-step purification, highly active enzyme (42 U/mg) was obtained using moderately hydrophobic ligand (octyl). The crude enzyme immobilized on octyl gel by adsorption showed significant operational stability over a period of 30 d at room temperature. Reactor studies demonstrated the feasibility of hydrophobic ligands as a medium for immobilization.

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Authors and Affiliations

  1. Chemical Engineering Division, National Chemical Laboratory, 411 008, Pune, India

    Harshvardhan V. Adikane, Rajesh K. Singh, Dnyaneshwar M. Thakar & Sanjay N. Nene

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  1. Harshvardhan V. Adikane
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  2. Rajesh K. Singh
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  3. Dnyaneshwar M. Thakar
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  4. Sanjay N. Nene
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Correspondence to Harshvardhan V. Adikane.

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Adikane, H.V., Singh, R.K., Thakar, D.M. et al. Single-step purification and immobilization of penicillin acylase using hydrophobic ligands. Appl Biochem Biotechnol 94, 127–134 (2001). https://doi.org/10.1385/ABAB:94:2:127

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  • DOI: https://doi.org/10.1385/ABAB:94:2:127

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