Purkarthofer Thomas, Skranc Wolfgang, Schuster Christian, Griengl Herfried
Research Centre Applied Biocatalysis, Petersgasse 14, 8010 Graz, Austria.
Appl Microbiol Biotechnol. 2007 Aug;76(2):309-20. doi: 10.1007/s00253-007-1025-6. Epub 2007 Jul 3.
The application of hydroxynitrile lyases (HNLs) as catalysts for the stereoselective condensation of HCN with carbonyl compounds has been reported as early as 1908. This enzymatic C-C bond coupling reaction furnishes enantiopure cyanohydrins which serve as versatile bifunctional building blocks for chemical synthesis. Screening of natural sources led to the discovery of both (R)- and (S)-selective HNLs, and several distinctly different classes of these enzymes with substantial differences concerning sequence, structure, and mechanism have been found. Especially during the last two centuries, HNLs have been developed into valuable biocatalysts, which can be produced in recombinant form by overexpression in microbial hosts, resulting in the implementation of industrial processes utilizing these enzymes. Recently, protein engineering in combination with in silico methods gave rise to the development of a tailor-made HNL for large-scale manufacturing of a specific target cyanohydrin.
早在1908年就有关于使用羟基腈裂解酶(HNLs)作为催化剂催化HCN与羰基化合物进行立体选择性缩合反应的报道。这种酶促碳 - 碳键偶联反应可生成对映体纯的氰醇,它们是化学合成中通用的双功能结构单元。对天然来源的筛选导致了(R) - 和(S) - 选择性HNLs的发现,并且已经发现了几类明显不同的这类酶,它们在序列、结构和机制方面存在显著差异。特别是在过去两个世纪中,HNLs已发展成为有价值的生物催化剂,可以通过在微生物宿主中过表达以重组形式生产,从而实现了利用这些酶的工业过程。最近,蛋白质工程与计算机方法相结合,开发出了一种定制的HNL,用于大规模生产特定的目标氰醇。