The advantage of this new group of polyesters over the traditional ones was that they were degradable by microorganisms at significant rates. Moreover, these results indicate that arylesterases could be an interesting enzyme class for identifications of polyesterases.īiodegradable polyesters were introduced to the markets in the 1980s due to the increasing amounts of polyesters ending up as waste in garbage dumps and the fact that these very stable compounds hydrolyse very slowly.
This is the first report of a PBAT degrading enzyme being identified by proteomic screening and shows that this approach can contribute to the discovery of new polymer hydrolysing enzymes. Modelling of an aromatic polyester mimicking oligomer into the PpEst active site indicated that the binding pocket could be big enough to accommodate large polymers. PpEst showed polyesterase activity on both whole and milled PBAT film releasing terephthalic acid and 4-(4-hydroxybutoxycarbonyl)benzoic acid while end product inhibition by 4-(4-hydroxybutoxycarbonyl)benzoic acid was observed.
PpEst was induced by the presence of PBAT in the growth media and had predicted arylesterase (EC 3.1.1.2) activity. A novel esterase, PpEst, that hydrolyses the co-aromatic-aliphatic polyester poly(1,4-butylene adipate-co-terephthalate) (PBAT) was identified by proteomic screening of the Pseudomonas pseudoalcaligenes secretome.
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