Probing batch and continuous flow reactions in organic solvents: Granulicella tundricola hydroxynitrile lyase (GtHNL)

José Coloma,Peter-Leon Hagedoorn,Yann Guiavarc'H,Ulf Hanefeld

doi:10.1039/d0cy00604a

Abstract

Granulicella tundricola hydroxynitrile lyase (GtHNL) is a manganese dependent cupin which catalyses the enantioselective synthesis of (R)-cyanohydrins.

Highlights

Enzyme catalysed carbon–carbon bond forming reactions are important in organic chemistry to produce chiral compounds.[1,2] In plants, hydroxynitrile lyases (HNLs) catalyse the cleavage of cyanohydrins into aldehydes or ketones releasing toxic hydrogen cyanide (HCN)
We describe the immobilisation of GtHNLTV on Celite R-633, the silicate skeletons of diatoms,[12] for the synthesis of (R)-mandelonitrile in batch and continuous flow systems
Prunus amygdalus HNL (PaHNL) immobilised on Celite was compared to Avicel,[39] controlled pore glass and Sephadex,[17] in all cases Celite was the best carrier in terms of enzymatic activity

Summary

Introduction

Enzyme catalysed carbon–carbon bond forming reactions are important in organic chemistry to produce chiral compounds.[1,2] In plants, hydroxynitrile lyases (HNLs) catalyse the cleavage of cyanohydrins into aldehydes or ketones releasing toxic hydrogen cyanide (HCN). This mechanism is a defense system against the attack of predators (cyanogenesis) and a source of nitrogen for the biosynthesis of L-asparagine (nitrogen fixation).[3,4] The reverse reaction is of great interest as it enables the synthesis of chiral α-cyanohydrins (Scheme 1). Mn2+ was bound more tightly in the triple variant than in the wild type enzyme, which resulted in higher stability and activity

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Conclusion