Bioprospecting for polyesterase activity relevant for PET degradation in marine Enterobacterales isolates

Author:

Galarza–Verkovitch Denisse1,Turak Onur1,Wiese Jutta1,Rahn Tanja1,Hentschel Ute12,Borchert Erik1

Affiliation:

1. GEOMAR Helmholtz Centre for Ocean Research Kiel, Kiel, Schleswig-Holstein, Germany

2. Christian-Albrechts University of Kiel, Kiel, Schleswig-Holstein, Germany

Abstract

<abstract> <p>Plastics have quickly become an integral part of modern life. Due to excessive production and improper waste disposal, they are recognized as contaminants present in practically all habitat types. Although there are several polymers, polyethylene terephthalate (PET) is of particular concern due to its abundance in the environment. There is a need for a solution that is both cost-effective and ecologically friendly to address this pollutant. The use of microbial depolymerizing enzymes could offer a biological avenue for plastic degradation, though the full potential of these enzymes is yet to be uncovered. The purpose of this study was to use (1) plate-based screening methods to investigate the plastic degradation potential of marine bacteria from the order Enterobacterales collected from various organismal and environmental sources, and (2) perform genome-based analysis to identify polyesterases potentially related to PET degradation. 126 bacterial isolates were obtained from the strain collection of RD3, Research Unit Marine Symbioses-GEOMAR-and sequentially tested for esterase and polyesterase activity, in combination here referred to as PETase–like activity. The results show that members of the microbial families <italic>Alteromonadaceae</italic>, <italic>Shewanellaceae</italic>, and <italic>Vibrionaceae</italic>, derived from marine sponges and bryozoans, are the most promising candidates within the order Enterobacterales. Furthermore, 389 putative hydrolases from the α/β superfamily were identified in 23 analyzed genomes, of which 22 were sequenced for this study. Several candidates showed similarities with known PETases, indicating underlying enzymatic potential within the order Enterobacterales for PET degradation.</p> </abstract>

Publisher

American Institute of Mathematical Sciences (AIMS)

Subject

Microbiology (medical),Microbiology

Reference91 articles.

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