ArticleActa naturae
Stabilization of Transaminases in Aqueous-Organic Media by Pyridoxal-5'-phosphate: A Case Study of Transaminase from Desulfomonile tiedjei.
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Abstract
Pyridoxal-5'-phosphate (PLP)-dependent transaminases are highly efficient biocatalysts for the stereoselective synthesis of chiral amines, which are key building blocks in pharmaceuticals and chemical manufacturing. Fundamental research on enzymatic transamination includes the classical works of Alexander Braunstein, who discovered the transamination reaction; David Metzler, who studied the spectral properties of PLP-dependent enzymes; Esmond Snell, who investigated the kinetics of PLP-dependent enzymes; as well as studies by other Russian and international researchers. Despite extensive studies on PLP-dependent transaminases, their practical application remains limited. In addition to the unfavorable equilibrium of the transamination reaction and the narrow substrate specificity of transaminases, their stability under manufacturing conditions is a major constraint. Transaminase stability encompasses not only the structural integrity of the protein globule, but also the enzyme's ability to retain the PLP cofactor. PLP dissociation leads to enzyme inactivation and termination of the reaction. Modern biocatalytic processes are predominantly designed for aqueous-organic media to increase the solubility of hydrophobic substrates to hundreds of grams per liter. Under these conditions, the stability of transaminases, as with other enzymes, decreases. In the context of these challenges, this work investigates the efficiency of PLP binding as a factor in stabilizing the active holoenzyme of the transaminase from
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