Abstract
Depsidone ether hydrolase, an enzyme which hydrolases physodic acid to 5′-hydroxyolivetoric acid, has been purified 73-fold from crude extracts obtained from Pseudevernia furfuracea thalli. The enzyme has been entrapped in polyacrylamide gel matrices. This entrapment shows to increase the affinity of the enzyme for its substrate. Soluble depsidone ether hydrolase is completely inactivated at 6°C for 15 min whereas the immobilized enzyme retains about 43% of the initial activity after 15 min at 70°C. Entrapped enzyme retains about 90% of its initial activity after storage for 56 days at 25°C.
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