A New Thermophilic Ene-Reductase from the Filamentous Anoxygenic Phototrophic Bacterium Chloroflexus aggregans

Robescu, Marina Simona; Niero, Mattia; Loprete, Giovanni; Cendron, Laura; Bergantino, Elisabetta

doi:10.3390/microorganisms9050953

Open AccessArticle

A New Thermophilic Ene-Reductase from the Filamentous Anoxygenic Phototrophic Bacterium Chloroflexus aggregans

by

Marina Simona Robescu

,

Mattia Niero

,

Giovanni Loprete

,

Laura Cendron

^*

and

Elisabetta Bergantino

^*

Department of Biology, University of Padova, Viale G. Colombo 3, 35131 Padova, Italy

^*

Authors to whom correspondence should be addressed.

Microorganisms 2021, 9(5), 953; https://doi.org/10.3390/microorganisms9050953

Submission received: 7 April 2021 / Revised: 23 April 2021 / Accepted: 27 April 2021 / Published: 28 April 2021

(This article belongs to the Special Issue Microbial Extremophiles as Life Pioneers and Wellsprings of Valuable Molecules)

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Abstract

Aiming at expanding the biocatalytic toolbox of ene-reductase enzymes, we decided to explore photosynthetic extremophile microorganisms as unique reservoir of (new) biocatalytic activities. We selected a new thermophilic ene-reductase homologue in Chloroflexus aggregans, a peculiar filamentous bacterium. We report here on the functional and structural characterization of this new enzyme, which we called CaOYE. Produced in high yields in recombinant form, it proved to be a robust biocatalyst showing high thermostability, good solvent tolerance and a wide range of pH optimum. In a preliminary screening, CaOYE displayed a restricted substrate spectrum (with generally lower activities compared to other ene-reductases); however, given the amazing metabolic ductility and versatility of Chloroflexus aggregans, further investigations could pinpoint peculiar chemical activities. X-ray crystal structure has been determined, revealing conserved features of Class III (or thermophilic-like group) of the family of Old Yellow Enzymes: in the crystal packing, the enzyme was found to assemble as dimer even if it behaves as a monomer in solution. The description of CaOYE catalytic properties and crystal structure provides new details useful for enlarging knowledge, development and application of this class of enzymes.

Keywords: ene-reductases; photosynthetic extremophiles; thermophilic-like old yellow enzymes; Chloroflexus aggregans

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MDPI and ACS Style

Robescu, M.S.; Niero, M.; Loprete, G.; Cendron, L.; Bergantino, E. A New Thermophilic Ene-Reductase from the Filamentous Anoxygenic Phototrophic Bacterium Chloroflexus aggregans. Microorganisms 2021, 9, 953. https://doi.org/10.3390/microorganisms9050953

AMA Style

Robescu MS, Niero M, Loprete G, Cendron L, Bergantino E. A New Thermophilic Ene-Reductase from the Filamentous Anoxygenic Phototrophic Bacterium Chloroflexus aggregans. Microorganisms. 2021; 9(5):953. https://doi.org/10.3390/microorganisms9050953

Chicago/Turabian Style

Robescu, Marina Simona, Mattia Niero, Giovanni Loprete, Laura Cendron, and Elisabetta Bergantino. 2021. "A New Thermophilic Ene-Reductase from the Filamentous Anoxygenic Phototrophic Bacterium Chloroflexus aggregans" Microorganisms 9, no. 5: 953. https://doi.org/10.3390/microorganisms9050953

APA Style

Robescu, M. S., Niero, M., Loprete, G., Cendron, L., & Bergantino, E. (2021). A New Thermophilic Ene-Reductase from the Filamentous Anoxygenic Phototrophic Bacterium Chloroflexus aggregans. Microorganisms, 9(5), 953. https://doi.org/10.3390/microorganisms9050953

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A New Thermophilic Ene-Reductase from the Filamentous Anoxygenic Phototrophic Bacterium Chloroflexus aggregans

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