The production of primary amines is a topic of great interest, as these molecules are known to be a building block for pharmaceuticals and fine chemicals. Therefore, the enzymatic synthesis of 5-hydroxymethyl-2-furfuryl amine (HMFA) from biobased 5-(hydroxymethyl)furfural (HMF) is interesting as furfurals serve as important building blocks and can be produced from renewable resources. In this study, the amine transaminase from Silicibacter pomeroyi (SpATA) was used as soluble and immobilized catalyst on glutaraldehyde functionalized HA-beads (HAGA-Beads) to analyze and improve the HMFA synthesis. The HMF concentration was increased up to 900 mm for the soluble and 150 mm for the immobilized enzyme, achieving almost complete conversion. In addition, different molar excesses of the amine donor monoisopropylamine (MIPA) or l-Alanine (1x–100x) were assessed, to allow efficient HMFA synthesis and avoid unnecessary high concentrations. Furthermore, the reaction was finally upscaled to a 200 mL process using the SpinChem rotating bed reactor, reaching in the first cycle 93% conversion and producing 2.34 g of HMFA in 48 h, and 7 g HMFA over a total of five cycles.