Biocatalytic routes have gained considerable attention in the last decades as potentially effective and sustainable alternatives. Remarkably, amine transaminases (TAs) catalyse the direct synthesis of chiral amines from pro-chiral ketones, using cheap and readily available amino donors (e.g. amino-acids) through transamination, with excellent enantioselectivity and in mild conditions. TAs are catching the eye as tremendous achievements have been made recently, both at the fundamental and applied levels . Industrial applications of biocatalytic transamination, however, remain scarce for TAs are usually employed as free enzymes in solution, which display limited stability. Batch processes utilizing such free enzymes do not allow easy catalyst separation, recovery, and reuse . Thus, immobilization strategies are often proposed . Additionally, thermodynamic limitations and substrate/product inhibitions tend to limit the applicability of transaminases in asymmetric synthesis of enantiopure amines .