Covalently immobilize crude d-amino acid transaminase onto UiO-66-NH(2) surface for d-Ala biosynthesis.

Affiliation

Wang B(1), Zhou J(1), Zhang XY(1), Yang YS(2), Liu CH(3), Zhu HL(4), Jiao QC(5).
Author information:
(1)School of Life Sciences, Nanjing University, Nanjing 210023, China; State Key Laboratory of Pharmaceutical Biotechnology, Nanjing University, Nanjing 210023, China.
(2)Hi-Teching.Co.Ltd, Zhenjiang 212415, China. Electronic address: [Email]
(3)School of Life Sciences, Nanjing University, Nanjing 210023, China; State Key Laboratory of Pharmaceutical Biotechnology, Nanjing University, Nanjing 210023, China. Electronic address: [Email]
(4)School of Life Sciences, Nanjing University, Nanjing 210023, China; State Key Laboratory of Pharmaceutical Biotechnology, Nanjing University, Nanjing 210023, China. Electronic address: [Email]
(5)School of Life Sciences, Nanjing University, Nanjing 210023, China. Electronic address: [Email]

Abstract

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.