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Reducing enzyme conformational flexibility by multi-point covalent immobilisation
Authors:R Fernandez-Lafuente  A N P Wood  D A Cowan
Institution:(1) Department of Biochemistry and Molecular Biology, University College, London, UK
Abstract:Summary A thermostable esterase was immobilised to glyoxyl-agarose under conditions designed to generate ldquolimited-linkagerdquo and ldquomulti-pointrdquo covalent derivatives. The multi-point derivative was 830-fold more thermostable than the limited-linkage derivative and retained more activity in the presence of sodium chloride and organic solvents. Medium chain (C8) aliphatic p-nitrophenyl ester substrates, which inactivate the soluble enzyme, were shown to be more readily hydrolysed. Together these data support the contention that multi-point covalent immobilisation results in a more rigid, less conformationally flexible protein structure.
Keywords:
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