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Highly active enzyme–metal nanohybrids synthesized in protein–polymer conjugates

Nature Catalysis volume 2, pages 718–725 (2019)Cite this article

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Abstract

Building a bridge between enzymatic and heterogeneous catalysis provides new cascade industrial processes for manufacturing. However, the reaction conditions of enzymatic and heterogeneous catalysis mutually cause deactivation of catalysts. Here, we overcame this challenge by developing a special protocol for the synthesis of hybrid catalysts. We utilized protein–polymer nanoconjugates as confined nanoreactors for the in situ synthesis of lipase–palladium (Pd) nanohybrids. The 0.8 nm Pd nanoparticles exhibited increased activity in racemization of (S)-1-phenylethylamine. At 55 °C, which matches the optimum temperature of lipase, the activity is more than 50 times that of commercial Pd/C. It was found that the Pd–O coordination in Pd subnanoclusters contributed to the high activity. In the dynamic kinetic resolutions of pharmaceutical intermediates (±)-1-phenylethylamine, (±)-1-aminoindan and (±)-1,2,3,4-tetrahydro-1-naphthylamine, the lipase–Pd nanohybrids displayed 7.6, 3.1 and 5.0 times higher efficiencies than the combination of commercial immobilized lipase Novozym 435 and Pd/C. The lipase–Pd nanohybrids can be reused without agglomeration and activity loss.

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Fig. 1: Fabrication and characterization of Pd/CALB-P nanohybrids.
Fig. 2: Size and activity of Pd/CALB-P nanohybrids.
Fig. 3: Analysis of the coordination of Pd.
Fig. 4: Theoretical modelling of the origin of the high activity of Pd subnanoclusters in Pd/CALB-P.
Fig. 5: The catalytic performance and reusability of 0.8Pd/CALB-P nanohybrids for the DKR of 1-PEA.

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The data that support the plots within this paper and other findings of this study are available from the corresponding author upon request.

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Acknowledgements

This work was supported by the National Key Research and Development Plan of China (2016YFA0204300), the National Natural Science Foundation of China (21622603, 21878174 and 51573085) and the Beijing Natural Science Foundation (JQ18006). The authors thank beamline BL14W1 (Shanghai Synchrotron Radiation Facility) for providing the beam time.

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Author notes

  1. These authors contributed equally: Xiaoyang Li, Yufei Cao, Kai Luo.

Authors and Affiliations

  1. Key Lab for Industrial Biocatalysis, Ministry of Education, Department of Chemical Engineering, Tsinghua University, Beijing, China

    Xiaoyang Li, Yufei Cao, Yunze Sun, Jiarong Xiong, Licheng Wang, Zheng Liu & Jun Ge

  2. Department of Chemistry, Fudan University, Jiangwan Campus, Shanghai, China

    Kai Luo & Richard N. Zare

  3. Department of Chemistry, Tsinghua University, Beijing, China

    Jun Li & Hai Xiao

  4. Shanghai Synchrotron Radiation Facilities, Shanghai Institute of Applied Physics, Chinese Academy of Sciences, Shanghai, China

    Jingyuan Ma

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Contributions

J.G., H.X. and R.N.Z. supervised the project. J.G. and X.L. conceived the idea. X.L. performed the experiments with technical help from Y.S. and J.X. Y.C performed the calculations. K.L. performed the mass spectra analyses. J.M., Z.L. and J.L. participated in analysing the results. X.L., L.W., J.G., H.X. and R.N.Z. co-wrote the paper.

Corresponding authors

Correspondence to Jun Ge, Hai Xiao or Richard N. Zare.

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Supplementary Information

Supplementary Information

Supplementary Methods, Supplementary Tables 1–10, Supplementary Figs. 1–52 and Supplementary References

Supplementary Data 1

Cartesian coordinates Pd_111_phenylethylamine

Supplementary Data 2

Cartesian coordinates Pd_111_imine

Supplementary Data 3

Cartesian coordinates Pd/(1/1/1)_partial_oxidation_phenylethylamine

Supplementary Data 4

Cartesian coordinates Pd/(1/1/1)_partial_oxidation_imine

Supplementary Data 5

Cartesian coordinates CALB_Pluronic_initial

Supplementary Data 6

Cartesian coordinates CALB_Pluronic_final

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Li, X., Cao, Y., Luo, K. et al. Highly active enzyme–metal nanohybrids synthesized in protein–polymer conjugates. Nat Catal 2, 718–725 (2019). https://doi.org/10.1038/s41929-019-0305-8

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