Functional characterization of salt‐tolerant microbial esterase WDEst17 and its use in the generation of optically pure ethyl (<i>R</i>)‐3‐hydroxybutyrate

Wang, Yilong; Xu, Yan; Zhang, Yun; Sun, Aijun; Y, Hu

doi:10.1002/chir.22847

Cited by 9 publications

(5 citation statements)

References 34 publications

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“…Recent examples of biocatalysts that have been uncovered using a genome mining-based approach include a thermostable monoacylglycerol lipase from a deep-sea Geobacillus sp. ( Tang et al, 2019 ) and a salt-tolerant, enantio-selective esterase from the actinobacterium Dactylosporangium aurantiacum that generated optically pure (R)-3-hydroxybutyrate ( Wang et al, 2018 ).…”

Section: Resultsmentioning

confidence: 99%

Identification of BgP, a Cutinase-Like Polyesterase From a Deep-Sea Sponge-Derived Actinobacterium

et al. 2022

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Many marine bacteria produce extracellular enzymes that degrade complex molecules to facilitate their growth in environmental conditions that are often harsh and low in nutrients. Marine bacteria, including those inhabiting sea sponges, have previously been reported to be a promising source of polyesterase enzymes, which have received recent attention due to their potential ability to degrade polyethylene terephthalate (PET) plastic. During the screening of 51 marine bacterial isolates for hydrolytic activities targeting ester and polyester substrates, a Brachybacterium ginsengisoli B129SM11 isolate from the deep-sea sponge Pheronema sp. was identified as a polyesterase producer. Sequence analysis of genomic DNA from strain B129SM11, coupled with a genome “mining” strategy, allowed the identification of potential polyesterases, using a custom database of enzymes that had previously been reported to hydrolyze PET or other synthetic polyesters. This resulted in the identification of a putative PET hydrolase gene, encoding a polyesterase-type enzyme which we named BgP that shared high overall similarity with three well-characterized PET hydrolases—LCC, TfCut2, and Cut190, all of which are key enzymes currently under investigation for the biological recycling of PET. In silico protein analyses and homology protein modeling offered structural and functional insights into BgP, and a detailed comparison with Cut190 revealed highly conserved features with implications for both catalysis and substrate binding. Polyesterase activity was confirmed using an agar-based polycaprolactone (PCL) clearing assay, following heterologous expression of BgP in Escherichia coli. This is the first report of a polyesterase being identified from a deep-sea sponge bacterium such as Brachybacterium ginsengisoli and provides further insights into marine-derived polyesterases, an important family of enzymes for PET plastic hydrolysis. Microorganisms living in association with sponges are likely to have increased exposure to plastics and microplastics given the wide-scale contamination of marine ecosystems with these plastics, and thus they may represent a worthwhile source of enzymes for use in new plastic waste management systems. This study adds to the growing knowledge of microbial polyesterases and endorses further exploration of marine host-associated microorganisms as a potentially valuable source of this family of enzymes for PET plastic hydrolysis.

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Section: Resultsmentioning

confidence: 99%

Identification of BgP, a Cutinase-Like Polyesterase From a Deep-Sea Sponge-Derived Actinobacterium

et al. 2022

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“…Further introduction of cinchonidine stabilizer during the preparation of Rh NPs significantly improved the catalytic hydrogenation activity, but the ee was still rather low (Table , entry 2). In some previous heterogeneous enantioselective catalysis reports, the solvent used often have significant effect on the reactivity and enantioselectivity. To further optimize catalytic activity and enantioselectivity, we attempted to introduce cosolvent into the catalytic system (Table , entries 3‐8).…”

Section: Resultsmentioning

confidence: 99%

Enantioselective hydrogenation of α‐ketoesters catalyzed by cinchona alkaloid stabilized Rh nanoparticles in ionic liquid

Sun

2019

Chirality

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The heterogeneous enantioselective hydrogenation of α-ketoesters catalyzed by rhodium nanoparticles (Rh NPs) in ionic liquid was studied with the stabilization and modification of cinchona alkaloids. TEM characterization showed that well-dispersed Rh NPs of about 1.96 nm were obtained in ionic liquid. The results showed that cinchona alkaloids not only had good enantiodifferentiating ability but also accelerated the catalytic reaction.Under the optimum reaction conditions, the enantiomeric excess in ethyl benzoylformate hydrogenation could reach as high as 60.9%.

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“…A more recent example is a salt‐tolerant esterase identified and cloned from the same strain ( D. aurantiacum subsp. hamdenensis NRRL 18085) [76c] . The purified esterase, named WDEst17, could kinetically resolve racemic ethyl 3‐hydroxybutyrate to its R ‐isomer at a conversion rate of approximately 65 % and an excellent enantiomeric excess of 99 % after process optimization (Scheme V ).…”

Section: Stereo‐selective Reactions Catalyzed By Enzymes Derived From...mentioning

confidence: 99%

“…The purified esterase, named WDEst17, could kinetically resolve racemic ethyl 3‐hydroxybutyrate to its R ‐isomer at a conversion rate of approximately 65 % and an excellent enantiomeric excess of 99 % after process optimization (Scheme V ). The optically active R ‐isomer (ethyl R ‐3‐hydroxybutyrate) is a chiral intermediate for various compounds such as (+) ‐decarestrictine L [76c,78] …”

Section: Stereo‐selective Reactions Catalyzed By Enzymes Derived From...mentioning

confidence: 99%

Actinobacteria as Microbial Cell Factories and Biocatalysts in The Synthesis of Chiral Intermediates and Bioactive Molecules; Insights and Applications

Salama,

Mostafa,

Husseiny

et al. 2024

Chemistry & Biodiversity

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Actinobacteria are one of the most intriguing bacterial phyla in terms of chemical diversity and bioactivities of their reported biomolecules and natural products, including various types of chiral molecules. Actinobacterial genera such as Detzia, Mycobacterium, and Streptomyces are among the microbial sources targeted for selective reactions such as asymmetric biocatalysis catalyzed by whole cells or enzymes induced in their cell niche. Remarkably, stereoselective reactions catalyzed by actinobacterial whole cells or their enzymes include stereoselective oxidation, stereoselective reduction, kinetic resolution, asymmetric hydrolysis, and selective transamination, among others. Species of actinobacteria function with high chemo‐, regio‐, and enantio‐selectivity under benign conditions, which could help current industrial processing. Numerous selective enzymes were either isolated from actinobacteria or expressed from actinobacteria in other microbes and hence exploited in the production of pure organic compounds difficult to obtain chemically. In addition, different species of actinobacteria, especially Streptomyces species, function as natural producers of chiral molecules of therapeutic importance. Herein, we discuss some of the most outstanding contributions of actinobacteria to asymmetric biocatalysis, which are important in the organic and/or pharmaceutical industries. In addition, we highlight the role of actinobacteria as microbial cell factories for chiral natural products with insights into their various biological potentialities.

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Functional characterization of salt‐tolerant microbial esterase WDEst17 and its use in the generation of optically pure ethyl (R)‐3‐hydroxybutyrate

Cited by 9 publications

References 34 publications

Identification of BgP, a Cutinase-Like Polyesterase From a Deep-Sea Sponge-Derived Actinobacterium

Identification of BgP, a Cutinase-Like Polyesterase From a Deep-Sea Sponge-Derived Actinobacterium

Enantioselective hydrogenation of α‐ketoesters catalyzed by cinchona alkaloid stabilized Rh nanoparticles in ionic liquid

Actinobacteria as Microbial Cell Factories and Biocatalysts in The Synthesis of Chiral Intermediates and Bioactive Molecules; Insights and Applications

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