A Comprehensive Overview of Novel Hydroxynitrile Lyases

preprint OA: closed
View at publisher

Abstract

Hydroxynitrile lyases (HNLs) are a heterogeneous family of enzymes that are of particular interest because of their structurally unique categories, a wide range of immobilisation techniques and procedures, and a wide range of sources with varying degrees of enantiopurity and enantioselectivity. Cupin, which contains a new type of HNL from bacteria, the lipocalin superfamily, which has HNLs from millipedes, and the + barrel fold superfamily, which contains HNL from a fern, have all been discovered in recent decades. Their biochemistry has been deciphered, and engineering efforts have been made to boost their productivity, purity, and activity. These remarkable enzymes opened up a new vista in the field of industrial catalysts since they are actively used in the synthesis of crucially important agrochemicals, medicines, physiologically active substances, and chemo-enzymatic follow-up procedures. This review focuses on recent advances, evolutionary history, and recombinant engineering of HNL from the previous decade.

My notes (saved in your browser only)

Citation neighborhood (no data yet)

We don't have any in-corpus citations linked to this paper yet. The paper's references may be in our DB but unresolved to ``paper_id`` (resolution happens at ingest when the cited DOI matches a row we already have). Run the cross-source citation reconcile pass to retry.

Source provenance

europepmc
last seen: 2026-05-19T01:45:01.086888+00:00