Cross-linked stabilization of Escherichia coli penicillin G acylase against pH by dextran-dialdehyde polymers |
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| Authors: | Haluk Ertan Dilek Kazan Altan Erarslan |
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| Affiliation: | (1) Faculty of Science, Department of Biology Vezneciler, Istanbul University, 34459 Istanbul, Turkey;(2) Marmara Research Centre, Research Institute of Genetic Engineering and Biotechnology, The Scientific and Technical Research Council of Turkey, P.O. Box 21, 41470 Gebze-Kocaeli, Turkey;(3) Faculty of Art and Science, Department of Chemistry, Kocaeli University, 41300 Izmit-Kocaeli, Turkey |
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| Abstract: | The inactivation kinetics of Escherichia coli penicillin G acylase (PGA), and cross-linked stabilization of the enzyme by dextran-dialdehyde derivatives of molecular weights of 11500, 37000 and 71000, were similar from pH 2 to pH 10. Inactivation of the native and modified PGA obeyed first order kinetics. The lowest inactivation rate constants for native and dextran-11500-dialdehyde modified PGA were 9.0310 and 1.5310 min respectively at pH 7.0. The highest pH stabilization (nearly ten-fold) was obtained at pH 7.0. |
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