Abstract
IN recent years the chemical and physical properties of matrix-supported enzymes have received considerable attention in the chemical literature1,2. The discovery that biologically active compounds can be fixed artificially to insoluble polymeric supports has generated an interest in these materials which is manifest in their wide applicability to the study of complex biological systems. This is so because, in general, the immobilization of active proteins has been shown to produce several significant chemical and physical changes in the protein relative to its native-state counterpart. For example, certain enzymes, which in an isolated extracellular environment exhibit relatively low thermal stability, can be materially stabilized by attachment to an inert polymeric support. Furthermore, chemical properties, which are manifest in the mechanism of action, can be altered significantly by the technique, for example reaction kinetics and substrate specificity.
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BARTLING, G., BROWN, H. & CHATTOPADHYAY, S. Synthesis of a Matrix-supported Enzyme in Non-aqueous Conditions. Nature 243, 342–344 (1973). https://doi.org/10.1038/243342b0
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DOI: https://doi.org/10.1038/243342b0
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