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SHR Neuro Krebs Kardio Lipid

Wallace, PW; Haernvall, K; Ribitsch, D; Zitzenbacher, S; Schittmayer, M; Steinkellner, G; Gruber, K; Guebitz, GM; Birner-Gruenberger, R.
PpEst is a novel PBAT degrading polyesterase identified by proteomic screening of Pseudomonas pseudoalcaligenes.
Appl Microbiol Biotechnol. 2017; 101(6):2291-2303 [OPEN ACCESS]
Web of Science PubMed PUBMED Central FullText FullText_MUG

 

Autor/innen der Med Uni Graz:
Birner-Grünberger Ruth
Schittmayer-Schantl Matthias
Wallace Pal William
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Number of Figures: 5
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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.

Find related publications in this database (Keywords)
Proteomics
Poly(1,4-butylene adipate-co-terephthalate) (PBAT)
Secretome
Polymer degradation
Polyesterase
Arylesterase
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