Abstract
Lignin peroxidase immobilization was achieved by covalent coupling on CNBr-Sepharose 4B. Protein immobilization yield was around 80%. For veratryl alcohol oxidation, in the presence of hydrogen peroxide, both soluble and bound enzymes exhibited the same pH profile with an optimum near 2.5. Catalytic parameters (kc andK m ) were seriously affected by immobilization. On the other hand, immobilization provided a noticeable stabilization of the enzyme against acidic pH and high temperatures. A 15–20 increase in the half-inactivation times at pH 2.2 and 2.7, respectively, could be observed. Bound enzyme was also much more thermostable than soluble.
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Asther, M., Meunier, JC. Immobilization as a tool for the stabilization of lignin peroxidase produced byPhanerochaete chrysosporium INA-12. Appl Biochem Biotechnol 38, 57–67 (1993). https://doi.org/10.1007/BF02916412
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DOI: https://doi.org/10.1007/BF02916412