Immobilization of ω-transaminases by encapsulation in a sol-gel/celite matrix
ABSTRACT Commercially available ω-transaminases ω-TA-117, -113, and Vibrio fluvialis (Vf-AT) have been immobilized in a sol-gel matrix. Improved results were obtained by employing Celite 545 as additive. The immobilized ω-transaminases ω-TA-117, -113, and V. fluvialis (Vf-AT) were tested in the kinetic resolution of α-chiral primary amines. In contrast to the free enzyme ω-TA-117, the sol-gel/celite immobilized enzyme showed activity even at pH 11. Recycling of the sol-gel/Celite 545 immobilized ω-transaminase ω-TA-117 was performed over five reaction cycles without any substantial loss in enantioselectivity and conversion. Finally, the immobilized ω-TA 117 was employed in a one-pot two-step deracemization of rac-mexiletine and rac-4-phenyl-2-butylamine, two pharmacologically relevant amines. The corresponding optically pure (S)-amines were obtained in up to 95% isolated yield (>99% ee).
Article: Industrial BiotransformationsMolecules. 01/2001;
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ABSTRACT: The present state of enzyme catalysis and the prospects for its introduction in organic synthesis are examined. The physicochemical approaches whereby the yield of the desired product can be increased under conditions favourable for biocatalysis (at the optimum of the catalytic activity and stability of the enzyme) are analysed. Together with classical equilibrium and kinetic preparative methods, the thermodynamic features and general methodological aspects of a new approach — enzymatic synthesis in two-phase systems comprising water and a water-immiscible organic solvent — are discussed in detail. The bibliography includes 170 references.Russian Chemical Reviews 10/2007; 50(8):718. · 2.30 Impact Factor