Cover Feature: Modeling‐Assisted Design of Thermostable Benzaldehyde Lyases from Rhodococcus erythropolis for Continuous Production of α‐Hydroxy Ketones (ChemBioChem 7/2022)

The right tool can do the trick: A novel thermostable benzaldehyde lyase from Rhodococcus erythropolis was identified using the computer‐assisted prediction tool Tome, and two variants with altered active sites were constructed based on homology models. All new enzyme variants showed significantly increased thermostability compared with the only experimentally confirmed benzaldehyde lyase from Pseudomonas fluorescens to date. The enzyme variants showed different substrate specificities and different activities in the presence of a range of co‐solvents. The most stable variant was then immobilized and used for continuous production of enantiopure benzoin. More information can be found in the Full Paper by K. S. Rabe et al.