Mandelic acids are valuable products which are used in a broad field of applications. The enzyme hydroxymandelate synthase (HMS) is a non-heme iron dioxygenase which converts para-hydroxyphenylpyruvate and other 3-aryl pyruvates by decarboxylation to the corresponding mandelates. In the present work, the gene hms encoding the hydroxymandelate synthase from Amycolatopsis mediterranei was cloned and overexpressed in Escherichia coli BL21(DE3) for in vivo cascade catalysis taking advantage of resident aromatic amino acid transaminases. The resulting recombinant cells were used for whole cell biotransformations. We successfully accomplished the production of para-hydroxymandelate exclusively by using the aromatic amino acid l-tyrosine in biotransformation. Furthermore, by utilizing different phenylalanine derivatives (including chloro-, fluoro- and hydroxylated amino acids), the corresponding S-mandelic acids were obtained with high conversion (21–87 %) and high ee (38–97%). This process is an alternative and attractive way to get access to a variety of mandelic acids.

扁桃酸是有价值的产品，被广泛应用。酶hydroxymandelate合酶（HMS）是一个非血红素铁的双加氧酶，其将第脱羧-hydroxyphenylpyruvate等3-芳基丙酮酸盐到相应的扁桃酸盐。在目前的工作中，利用驻在芳香族氨基酸转氨酶，在大肠杆菌BL21（DE3）中克隆并过表达编码来自地中海扁桃的羟基扁桃酸合酶的基因hms，并在其中进行过表达。所得重组细胞用于全细胞生物转化。我们成功完成了para的制作-羟基扁桃酸酯仅通过在生物转化中使用芳香族氨基酸1-酪氨酸来实现。此外，通过利用不同的苯丙氨酸衍生物（包括氯代，氟代和羟基化氨基酸），可获得相应的S-扁桃酸，具有较高的转化率（21–87％）和较高的ee（38–97％）。此过程是获得各种扁桃酸的一种替代且有吸引力的方法。