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Appl Microbiol Biotechnol. 2017 Mar;101(6):2291-2303. doi: 10.1007/s00253-016-7992-8. Epub 2016 Nov 21.

PpEst is a novel PBAT degrading polyesterase identified by proteomic screening of Pseudomonas pseudoalcaligenes.

Author information

1
Research Unit for Functional Proteomics and Metabolic Pathways, Institute of Pathology, Medical University of Graz, Stiftingtalstrasse 24, 8010, Graz, Austria.
2
Austrian Centre of Industrial Biotechnology, Petersgasse 14, 8010, Graz, Austria.
3
Omics Center Graz, BioTechMed-Graz, Graz, Austria.
4
Austrian Centre of Industrial Biotechnology, Konrad Lorenz Strasse 20, 3430, Tulln, Austria.
5
Institute of Environmental Biotechnology, University of Natural Resources and Life Sciences, Konrad Lorenz Strasse 20, 3430, Tulln, Vienna, Austria.
6
Institute of Molecular Biosciences, University of Graz, Humboldtstraße 50/III, 8010, Graz, Austria.
7
Research Unit for Functional Proteomics and Metabolic Pathways, Institute of Pathology, Medical University of Graz, Stiftingtalstrasse 24, 8010, Graz, Austria. ruth.birner-gruenberger@medunigraz.at.
8
Austrian Centre of Industrial Biotechnology, Petersgasse 14, 8010, Graz, Austria. ruth.birner-gruenberger@medunigraz.at.
9
Omics Center Graz, BioTechMed-Graz, Graz, Austria. ruth.birner-gruenberger@medunigraz.at.

Abstract

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.

KEYWORDS:

Arylesterase; Poly(1,4-butylene adipate-co-terephthalate) (PBAT); Polyesterase; Polymer degradation; Proteomics; Secretome

PMID:
27872998
PMCID:
PMC5320007
DOI:
10.1007/s00253-016-7992-8
[Indexed for MEDLINE]
Free PMC Article

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