Covalently immobilize crude D-amino acid transaminase onto UiO-66-NH2 surface for D-Ala biosynthesis

Enzyme reaction has been accepted widely in numerous applications owing to the high efficiency and stereo-selectivity, as well as simple preparation by gene engineering. However, the fragility and complex purification process of the enzyme are long-standing problems which limit the large-scale application. One possible solution may be the enzyme immobilization. As one type of porous material with high loading capacity and designable functionality, Metal-Organic Frameworks (MOFs) are ideal choices for the immobilization of enzyme with a considerable interest in recent years. In this study, D-amino acid transaminase (DAT), an important enzyme for industrial synthesis of D-Ala, was covalently immobilized on the surface of a star MOFs material, UiO-66-NH2. Interestingly, we found that the nanoscale hybrid enzyme UiO-66-NH2-Gd-DAT not only maintained the high catalytic efficiency but also got rid of the interference of polluting enzymes, which meant that we could obtain efficient and stereo-selective immobilized enzyme without complex purification process. In general, our findings demonstrated that using UiO-66-NH2 might be a promising strategy to immobilize enzyme and produce effective biocatalyst with high activity and stereo-selectivity. (C) 2021 Elsevier B.V. All rights reserved.

Automated summary

Enzyme immobilization on Metal-Organic Frameworks (MOFs) provides a promising strategy to produce effective biocatalysts with high activity and stereo-selectivity. Covalently immobilizing D-amino acid transaminase (DAT) on UiO-66-NH2 allows for maintaining high catalytic efficiency and eliminating interference from contaminating enzymes, without the need for complex purification processes.