Proteomics

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Polyesterase discovery in Pseudomonas pseudoalcaligenes secretome


ABSTRACT: By screening the secretomes of polymer induced Pseudomonas pseudoalcaligenes we identify a new enzyme PpEst that can degrade the co-aliphatic-aromatic polyester poly(1,4-butylene adipate-co-terephthalate) (PBAT). The discovered enzyme has predicted arylesterase activity and is induced by PBAT added to the growth medium

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Pseudomonas Pseudoalcaligenes

SUBMITTER: Paal William Wallace  

LAB HEAD: Ruth Birner-gruenberger

PROVIDER: PXD004014 | Pride | 2016-12-13

REPOSITORIES: Pride

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Publications

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

Wallace Paal W PW   Haernvall Karolina K   Ribitsch Doris D   Zitzenbacher Sabine S   Schittmayer Matthias M   Steinkellner Georg G   Gruber Karl K   Guebitz Georg M GM   Birner-Gruenberger Ruth R  

Applied microbiology and biotechnology 20161121 6


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  ...[more]

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