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Physicochemical Aspects of Immobilized Enzyme-Matrix Interactions

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Enzyme Engineering

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Abstract

The utilization of immobilized enzymes as catalytic and regulating agents opens up vast possibilities for their application in medicine and chemical technology. On the other hand, immobilized enzymes are useful in the study of basic problems in biochemistry. The development of scientific principles relevant to the production of immobilized enzymes having high stability is a major concern of applied enzymology. Theoretically, the discovery of ways to stabilize enzymes would provide a basis for understanding the general mechanisms of protein denaturation which are still unknown (1,2). In addition, the determination of factors governing enzyme stability would answer a very important general question in biochemistry concerning the reasons why most purified enzymes have a lowered stability compared to enzymes in their natural environment (2). As a practical consequence the solution to this problem would make it possible to develop a general strategy for the synthesis of enzyme preparations suitable for long-term operation.

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Author information

Authors and Affiliations

  1. Department of Chemistry, M.V. Lomonosov Moscow State University, Moscow, USSR

    I. V. Berezin

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  1. I. V. Berezin
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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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Berezin, I.V. (1978). Physicochemical Aspects of Immobilized Enzyme-Matrix Interactions. In: Pye, E.K., Weetall, H.H. (eds) Enzyme Engineering. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-5163-5_14

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  • DOI: https://doi.org/10.1007/978-1-4757-5163-5_14

  • 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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