Journal
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
Volume 101, Issue 6, Pages 2291-2303Publisher
SPRINGER
DOI: 10.1007/s00253-016-7992-8
Keywords
Proteomics; Poly(1,4-butylene adipate-co-terephthalate) (PBAT); Secretome; Polymer degradation; Polyesterase; Arylesterase
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Funding
- Medical University of Graz (Graz, Austria)
- Austrian Science Fund (FWF) doctoral school 'DK Metabolic and Cardiovascular Disease' [W1226]
- Federal Ministry of Economy, Family and Youth (BMWFJ) [P26074]
- Federal Ministry of Traffic, Innovation and Technology (bmvit)
- Styrian Business Promotion Agency SFG
- Standortagentur Tirol and ZIT-Technology Agency of the City of Vienna through COMET
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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. PpEst was induced by the presence of PBAT in the growth media and had predicted arylesterase (EC 3.1.1.2) activity. 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. 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. 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. Moreover, these results indicate that arylesterases could be an interesting enzyme class for identifications of polyesterases.
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