Characterization of a novel thermostable (S)-amine-transaminase from an Antarctic moderately-thermophilic bacterium Albidovulum sp. SLM16

Márquez, Sebastián; Atalah, Joaquín; Blamey, Jenny M.

doi:10.1016/j.enzmictec.2019.109423

Cited by 13 publications

(13 citation statements)

References 60 publications

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“…This microorganism was identified as Albidovulum sp. SLM16, with optimal growth conditions at 55°C, pH 6.5–8.0, 1–3% NaCl ( Márquez and Blamey, 2019 ). A novel (S)-ATA enzyme was purified from the crude extract and biochemically characterized.…”

Section: Resultsmentioning

confidence: 99%

“…A novel (S)-ATA enzyme was purified from the crude extract and biochemically characterized. The recombinant version of this enzyme has been obtained with a purity of 99.7% ( Supplementary Table S1 ), and found to be active in a wide range of temperatures (20–70°C), showing optimal activity at 65°C and pH 9.5, with a remarkable thermostability maintaining 80% of its specific activity after 5 days of incubation at 50°C ( Marquez and Blamey, 2019 ).…”

Section: Resultsmentioning

confidence: 99%

“… - Thermophilic amine-transaminase producing microorganisms were screened in environmental samples collected from fumaroles located in Whalers Bay, Deception Island, Antarctica. Samples were cultivated at 50°C and pH 7.6 for 24 h in media supplemented with 10 mM α -methylbenzylamine (MBA) as an inductor of amine-transaminase activity ( Márquez and Blamey, 2019 ). …”

Section: Methodsmentioning

confidence: 99%

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From the Discovery of Extremozymes to an Enzymatic Product: Roadmap Based on Their Applications

Espina

Muñoz-Ibacache

Cáceres-Moreno

et al. 2022

Front. Bioeng. Biotechnol.

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With the advent of the industrial revolution, the use of toxic compounds has grown exponentially, leading to a considerable pollution of the environment. Consequently, the development of more environmentally conscious technologies is an urgent need. Industrial biocatalysis appears as one potential solution, where a higher demand for more robust enzymes aims to replace toxic chemical catalysts. To date, most of the commercially available enzymes are of mesophilic origin, displaying optimal activity in narrow ranges of temperature and pH (i.e., between 20°C and 45°C, neutral pH), limiting their actual application under industrial reaction settings, where they usually underperform, requiring larger quantities to compensate loss of activity. In order to obtain novel biocatalysts better suited for industrial conditions, an efficient solution is to take advantage of nature by searching and discovering enzymes from extremophiles. These microorganisms and their macromolecules have already adapted to thrive in environments that present extreme physicochemical conditions. Hence, extremophilic enzymes stand out for showing higher activity, stability, and robustness than their mesophilic counterparts, being able to carry out reactions at nonstandard conditions. In this brief research report we describe three examples to illustrate a stepwise strategy for the development and production of commercial extremozymes, including a catalase from an Antarctic psychrotolerant microorganism, a laccase from a thermoalkaliphilic bacterium isolated from a hot spring and an amine-transaminase from a thermophilic bacterium isolated from a geothermal site in Antarctica. We will also explore some of their interesting biotechnological applications and comparisons with commercial enzymes.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

From the Discovery of Extremozymes to an Enzymatic Product: Roadmap Based on Their Applications

Espina

Muñoz-Ibacache

Cáceres-Moreno

et al. 2022

Front. Bioeng. Biotechnol.

Self Cite

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“…SLM16. [19] Enzymes from extremophiles may have a huge practical potential thanks to their higher robustness, a property that could make them more suitable for industrial applications than their mesophilic counterparts. [20,21] In this work, we have exploited a culture enrichment approach to discover novel TAs, using different amines as selective medium and starting from samples collected in (hyper)thermophilic environments.…”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Discovery and Characterization of a Novel Thermostable β‐Amino Acid Transaminase from a Meiothermus Strain Isolated in an Icelandic Hot Spring

Ferrandi

Bassanini

Sechi

et al. 2020

Biotechnology Journal

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A Meiothermus strain capable of using β‐phenylalanine for growth is isolated by culture enrichment of samples collected in hot environments and the genome is sequenced showing the presence of 22 putative transaminase (TA) sequences. On the basis of phylogenetic and sequence analysis, a TA termed Ms‐TA2 is selected for further studies. The enzyme is successfully produced in Escherichia coli Rosetta(DE3) cells, with 70 mg of pure protein obtained from 1 L culture after purification by affinity chromatography. Ms‐TA2 shows high activity toward (S)‐β‐phenylalanine and other (S)‐β‐amino acids, as well as a preference for α‐ketoglutarate and aromatic aldehydes as amino acceptors. Moreover, Ms‐TA2 is shown to be a thermostable enzyme by maintaining about 60% of the starting activity after 3 h incubation at 50 °C and showing a melting temperature of about 73 °C. Finally, a homology‐based structural model of Ms‐TA2 is built and key active site interactions for substrate and cofactor binding are analyzed.

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Considerations for the Scale‐up of in vitro Transaminase‐Catalyzed Asymmetric Synthesis of Chiral Amines

Madsen

Woodley

2023

ChemCatChem

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In vitro transaminase catalyzed asymmetric synthesis is not a new phenomenon in the biocatalytic toolbox. Our group published a review on process consideration for these reactions in 2011, in which process metrics and the unfavorable reaction equilibrium was deduced to be the main bottlenecks at the time. Now, a decade later, this has been solved by different process methods presented in this review, with the development of enzymatic cascades one of the main solutions. Today, the new bottleneck is the downstream processing, due to the complexity of transaminase reactions, in which a ketone and an amine as substrates and a new ketone and a new amine as products. How to recover the produced amine from the resulting product mixture is considered and will be the key challenge for scale‐up of such systems in the near future.

show abstract

Characterization of a novel thermostable (S)-amine-transaminase from an Antarctic moderately-thermophilic bacterium Albidovulum sp. SLM16

Cited by 13 publications

References 60 publications

From the Discovery of Extremozymes to an Enzymatic Product: Roadmap Based on Their Applications

From the Discovery of Extremozymes to an Enzymatic Product: Roadmap Based on Their Applications

Discovery and Characterization of a Novel Thermostable β‐Amino Acid Transaminase from a Meiothermus Strain Isolated in an Icelandic Hot Spring

Considerations for the Scale‐up of in vitro Transaminase‐Catalyzed Asymmetric Synthesis of Chiral Amines

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