Journal Article

FZJ-2020-01079

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png A Novel Polyester Hydrolase From the Marine Bacterium Pseudomonas aestusnigri – Structural and Functional Insights

Bollinger, A.FZJ* ; Thies, S.FZJ* ; Knieps-Grünhagen, E.FZJ* ; Gertzen, C. ; Kobus, S. ; Höppner, A. ; Ferrer, M. ; Gohlke, H.FZJ* ; Smits, S. H. J. ; Jaeger, K.-E. (Corresponding author)FZJ*

2020
Frontiers Media Lausanne

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Please use a persistent id in citations: http://hdl.handle.net/2128/26914  doi:10.3389/fmicb.2020.00114

Abstract: Biodegradation of synthetic polymers, in particular polyethylene terephthalate (PET), is of great importance, since environmental pollution with PET and other plastics has become a severe global problem. Here, we report on the polyester degrading ability of a novel carboxylic ester hydrolase identified in the genome of the marine hydrocarbonoclastic bacterium Pseudomonas aestusnigri VGXO14T. The enzyme, designated PE-H, belongs to the type IIa family of PET hydrolytic enzymes as indicated by amino acid sequence homology. It was produced in Escherichia coli, purified and its crystal structure was solved at 1.09 Å resolution representing the first structure of a type IIa PET hydrolytic enzyme. The structure shows a typical α/β-hydrolase fold and high structural homology to known polyester hydrolases. PET hydrolysis was detected at 30°C with amorphous PET film (PETa), but not with PET film from a commercial PET bottle (PETb). A rational mutagenesis study to improve the PET degrading potential of PE-H yielded variant PE-H (Y250S) which showed improved activity, ultimately also allowing the hydrolysis of PETb. The crystal structure of this variant solved at 1.35 Å resolution allowed to rationalize the improvement of enzymatic activity. A PET oligomer binding model was proposed by molecular docking computations. Our results indicate a significant potential of the marine bacterium P. aestusnigri for PET degradation.

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Contributing Institute(s):

1. Institut für Molekulare Enzymtechnologie (HHUD) (IMET)

Research Program(s):

1. 581 - Biotechnology (POF3-581) (POF3-581)
2. DFG project 417919780 - Zentrum für strukturelle Studien (417919780)

Appears in the scientific report 2020

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Database coverage:
; ; ; ; BIOSIS Previews ; Clarivate Analytics Master Journal List ; DOAJ Seal ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; PubMed Central ; SCOPUS ; Science Citation Index Expanded ; Web of Science Core Collection

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