Continuous‑flow biocatalysis for cost‑effective UPO applications

For a study by Elena Gkantzou, Theofilia Koulopoulou, Anton Glieder, and Selin Kara, Aminoverse delivered AaeUPO for immobilisation and continuous‑flow biocatalysis in a 3D‑printed microfluidic reactor. AaeUPO retained about 94 % of its initial activity after immobilisation and still showed ~50 % activity after 20 cycles, with a space time yield of 2.1 g/(L·h) and a total turnover number > 19,000.

This combination of enzyme immobilisation and flow operation enables dramatic reductions in biocatalyst cost. Calculations based on a pyridine‐derivative transformation indicated that immobilised UPOs in continuous mode can reduce cost of goods sufficiently to achieve enzyme and reagent costs below 5$ per kg of product. Thus, UPOs become viable even for high-volume, low-margin chemical manufacturing.

Across industries—from fine chemicals to pharmaceuticals and specialty materials—the versatility of immobilised AaeUPO supports the synthesis of diverse products. This illustrates how Aminoverse UPOs in flow systems deliver scalable, sustainable biocatalysis with ultra‑low enzyme cost for broad industrial impact.

Unspecific peroxygenase immobilization in 3D-printed microfluidics: towards tailor-made screening platforms

“In the context of empowering biocatalysis, an easy-to-develop, reproducible, and easy-to-scale biocatalytic system under continuous flow is demonstrated. 3D printing technology is used as the reactor manufacturing method, yielding identical and low-cost microfluidic chips that can be further modified to serve as a biocatalytic platform for simultaneous parameter screening. The model enzyme studied here is unspecific peroxygenase (UPO). UPOs are currently under intensive study, due to their distinct promiscuity in oxyfunctionalization chemistry. This is the first study demonstrating UPO’s immobilization in a microfluidic concept. The developed method for surface functionalization of microfluidic reactors is based on polydopamine modification and was proven highly reproducible. UPO showed a TTN of 19 249 and a STY of 2.1 g L−1 h−1, under the specified conditions. The kinetic behavior of the system under flow conditions is reported. The system was also regenerated with a 51.4% recovered activity. Further utilization of microfluidic concepts is expected to unravel the full potential of UPOs for oxyfunctionalization reactions of particular interest. The proposed system is foreseen as a screening platform for different reaction conditions, reaction substrates, or enzyme mutants.”