Diffusion process in enzyme–metal hybrid catalysts

Abstract

Enzyme–metal hybrid catalysts bridge the gap between enzymatic and heterogeneous catalysis, which is significant for expanding biocatalysis to a broader scope. Previous studies have demonstrated that the enzyme–metal hybrid catalysts exhibited considerably higher catalytic efficiency in cascade reactions, compared with that of the combination of separated enzyme and metal catalysts. However, the precise mechanism of this phenomenon remains unclear. Here, we investigated the diffusion process in enzyme–metal hybrid catalysts using Pd/lipase-Pluronic conjugates and the combination of immobilized lipase (Novozyme 435) and Pd/C as models. With reference to experimental data in previous studies, the Weisz–Prater parameter and efficiency factor of internal diffusion were calculated to evaluate the internal diffusion limitations in these catalysts. Thereafter, a kinetic model was developed and fitted to describe the proximity effect in hybrid catalysts. Results indicated that the enhanced catalytic efficiency of hybrid catalysts may arise from the decreased internal diffusion limitation, size effect of Pd clusters and proximity of the enzyme and metal active sites, which provides a theoretical foundation for the rational design of enzyme–metal hybrid catalysts.

Graphical abstract

Keywords

enzyme–metal hybrid catalyst / internal diffusion / proximity effect / kinetic model

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Acknowledgements

This work was supported by the Beijing Natural Science Foundation (No. JQ18006), and the National Natural Science Foundation of China (Grant Nos. 21878174, 2191101041).

Electronic Supplementary Material

Supplementary material is available in the online version of this article at https://dx.doi.org/10.1007/s11705-022-2144-4 and is accessible for authorized users.

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