Tryptophan (Trp) analogues are a subgroup of noncanonical amino acids (ncAAs), which are increasingly valued in the chemical and pharmaceutical industries. Biocatalytic approaches to the preparation of enantiopure Trp analogues offer highly sustainable pathways with unrivalled stereoselectivity and efficiency. In this study, we characterized two novel TnaA enzymes from the extremophilic bacterium Ardenticatena maritima and archaeon Haloarcula japonica which, in comparison to the well-established Escherichia colitryptophanase (EcTnaA), exhibited enhanced stability under extreme physicochemical conditions, making them promising candidates for biocatalytic synthesis of indole-containing amino acids.

Wonderful collaboration with Alessandra Tolomelli and Ivano Eberini!

Well done to Roja and Evelyn, keep up the good work!

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