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The Immobilization of a Stable Esterase by Entrapment, Covalent Binding and Adsorption

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Enzyme Engineering

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Abstract

The deacetylation of cephalosporin C by B. subtilis (ATCC 6633) has been reported by Nüesch et al (1) several years ago. Since then we have isolated and partially characterized the intracellular esterase from this organism (2), and have immobilized it by several established techniques with a view to the laboratory application of the enzyme and also for the evaluation of the carriers and immobilization techniques. We report here some of the properties of the enzyme, the results of the immobilization studies and some of the properties of the immobilized preparations.

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References

  1. NIIESCH, J., GRUNER, J., KNÜSEL, F. & TREICHLER, H.J. Path. Microbial. 30: 880, 1967.

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Author information

Authors and Affiliations

  1. Pharmaceutical Division, CIBA-GEIGY LTD., Basel, Switzerland

    J. Konecny

Authors
  1. J. Konecny
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Editor information

Editors and Affiliations

  1. Department of Biochemistry and Biophysics School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, USA

    E. Kendall Pye

  2. Research and Development Labs, Corning Glass Works, Corning, New York, USA

    Howard H. Weetall

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© 1978 Springer Science+Business Media New York

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Konecny, J. (1978). The Immobilization of a Stable Esterase by Entrapment, Covalent Binding and Adsorption. In: Pye, E.K., Weetall, H.H. (eds) Enzyme Engineering. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-5163-5_2

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  • DOI: https://doi.org/10.1007/978-1-4757-5163-5_2

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4757-5165-9

  • Online ISBN: 978-1-4757-5163-5

  • eBook Packages: Springer Book Archive

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