Stabilization of transaminases in aqueous-organic media by pyridoxal-5’-phosphate: a case study of transaminase from <i>Desulfomonile tiedjei</i>

), both in incubation mode and under reaction conditions. Particular attention is paid to the analysis of the effect of the amino acid substitution T199Q in the cofactor-binding region on the enzyme's resistance to organic solvents. The present study contributes to addressing the practical problem of stabilizing transaminases in aqueous-organic media. The results also deepen our understanding of the molecular basis of the stability of PLP-dependent enzymes.

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Publication Details

Journal
Acta Naturae
Published
2026-04-21
DOI
https://doi.org/10.32607/actanaturae.27820
Primary Topic
Enzyme Catalysis and Immobilization
Type
article
Field-Weighted Citation Impact
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article

Stabilization of transaminases in aqueous-organic media by pyridoxal-5’-phosphate: a case study of transaminase from Desulfomonile tiedjei

I.V. Rudina, E. Yu. Bezsudnova, V. O. Popov, A. K. Bakunova
Acta Naturae
Enzyme Catalysis and Immobilization
article

Stabilization of transaminases in aqueous-organic media by pyridoxal-5’-phosphate: a case study of transaminase from Desulfomonile tiedjei

I.V. Rudina, E. Yu. Bezsudnova, V. O. Popov, A. K. Bakunova
article en

Abstract

), both in incubation mode and under reaction conditions. Particular attention is paid to the analysis of the effect of the amino acid substitution T199Q in the cofactor-binding region on the enzyme's resistance to organic solvents. The present study contributes to addressing the practical problem of stabilizing transaminases in aqueous-organic media. The results also deepen our understanding of the molecular basis of the stability of PLP-dependent enzymes.

Acta NaturaeVol. 18(1)
Russian Academy of Sciences (RU), Lomonosov Moscow State University (RU), Biotechnology Research Center (IR), Moscow State University (TJ)
Openalex Percentile: Top 19%
Enzyme Catalysis and Immobilization
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