Abstract
The kinetics of adsorption and hydrolysis by an extracellular PHB depolymerase from Alcaligenes faecalis were studied at 37°C on the surface of five types of polyhydroxyalkanoate (PHA) films. The films of poly[(R)-3-hydroxybutyrate](P(3HB)), poly(3-hydroxypropionate)(P(3HP)), and poly(4- hydroxybutyrate)(P(4HB)) were hydrolyzed by the enzyme, while the films of poly[(S)-2-hydroxypropionate)(P(2HP)) and poly(6-hydroxyhexanoate)(P(6HH)) were not eroded. The PHB depolymerase with binding and catalytic domains adsorbed on the surface of all PHA films used, and the adsorption kinetics were found to obey the Langmuir isotherm. The cross-area per one molecule of enzyme binding to the surface of PHA film was estimated to be 17 ± 8 (nm 2/molecule). It has been concluded that the binding domain of enzyme is non-specific for the binding to the surface of PHA films, while the active site in a catalytic domain is specific for the hydrolysis of PHA molecules
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