Hybrid enzyme catalysts synthesized by a de novo approach for expanding biocatalysis

doi:10.1016/S1872-2067(21)63798-1

Chinese Journal of Catalysis ›› 2021, Vol. 42 ›› Issue (10): 1625-1633.DOI: 10.1016/S1872-2067(21)63798-1

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Hybrid enzyme catalysts synthesized by a de novo approach for expanding biocatalysis

Yufei Cao^a, Jun Ge^a^,^b()

^aKey Lab for Industrial Biocatalysis, Ministry of Education, Department of Chemical Engineering, Tsinghua University, Beijing 100084, China
^bInstitute of Biopharmaceutical and Health Engineering, Tsinghua Shenzhen International Graduate School, Shenzhen 518055, Guangdong, China

Received:2021-02-07 Accepted:2021-03-04 Online:2021-06-20 Published:2021-04-25
Contact: Jun Ge
About author:Professor Jun Ge (Department of Chemical Engineering, Tsinghua University) received his B.S. degree in 2004 and Ph.D degree in 2009 from Tsinghua University. From 2009 to 2012, he did postdoctoral research at Stanford University. In 2012, he joined the faculty of Department of Chemical Engineering, Tsinghua University. His research interests currently focus on enzymatic catalysis and enzyme-metal cooperative catalysis with emphasis on design of new biocatalysts, enzyme catalyst engineering and asymmetric synthesis of pharmaceutical intermediates and fine chemicals by biocatalysis. Some of his recent progresses include the design of novel hybrid catalyst to combine lipase and Pd clusters to achieve the dynamic kinetic resolution of amines, the novel approach of enzymatic catalysis in cells to achieve the detection of specific intracellular metabolites in single cells. He has coauthored about 60 peer-reviewed papers, some of which were published in Nature Catalysis, Nature Nanotechnology, Science Advances, Nature Communications, etc. He has been issued with 10 patents. He joined the editorial board of Chin. J. Catal. as the Associate Editor in 2020.
Supported by:
Beijing Natural Science Foundation(JQ18006);National Key Research and Development Plan of China(2016YFA0204300);National Natural Science Foundation of China(21622603);National Natural Science Foundation of China(21878174);National Natural Science Foundation of China(21911540467)

Abstract

Abstract: The two major challenges in industrial enzymatic catalysis are the limited number of chemical reaction types that are catalyzed by enzymes and the instability of enzymes under harsh conditions in industrial catalysis. Expanding enzyme catalysis to a larger substrate scope and greater variety of chemical reactions and tuning the microenvironment surrounding enzyme molecules to achieve high enzyme performance are urgently needed. In this account, we focus on our efforts using the de novo approach to synthesis hybrid enzyme catalysts that can address these two challenges and the structure-function relationship is discussed to reveal the principles of designing hybrid enzyme catalysts. We hope that this account will promote further efforts toward fundamental research and wide applications of designed enzyme hybrid catalysts for expanding biocatalysis.

Key words: Expanding biocatalysis, In situ synthesis, Hybrid enzyme catalysts, Structure-function relationship, Rational design

Yufei Cao, Jun Ge. Hybrid enzyme catalysts synthesized by a de novo approach for expanding biocatalysis[J]. Chinese Journal of Catalysis, 2021, 42(10): 1625-1633.

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Figures/Tables 4

Fig. 1. (A) Single enzyme molecules are encapsulated in nanogels by surface acryloylation of a protein molecule followed by aqueous in situ polymerization. (B) Based on the analysis of enzyme sequences and the characteristic chemical patterns on enzyme surfaces, four-monomer random heteropolymers to mimic intrinsically disordered proteins are designed for enzyme solubilization and stabilization in nonnative environments. Reproduced with permission [18]. Copyright 2018, American Association for the Advancement of Science. (C) Enzyme molecules are directly embedded in inorganic crystals by a coprecipitation method. (D) In situ generation of Pd nanoparticles/clusters in a confined environment of a single lipase-polymer conjugate.

Fig. 2. (A) Scanning electron microscopy (SEM) images of calcinated Cyt c@ZIF-8. (B) The relative peroxidase activities of Cyt c, Cyt c@ZIF-8 composite, PVP/Cyt c mixture, Cyt c/zinc ion mixture, Cyt c/2-methylimidazole mixture, and Cyt c/ZIF-8 mixture. Reproduced with permission [21]. Copyright 2014, American Chemical Society. (C) NU-1000 encapsulation changes the coordination of the Cyt c heme active site. Probability distributions, P(D), of the N (His 18), S (Met 80), and C (Pro 30) distances relative to Fe in bulk. (D) Corresponding probability distributions inside MOF NU-1000. (E) The configurations of Cyt c in water. (F) The configurations of Cyt c inside MOF NU-1000. Reproduced with permission [23]. Copyright 2020, American Chemical Society. (G) Schematic illustration of the enzymatic cascade catalyzed by GOx/HRP@ZIF-8. (H) The relative overall activity of the enzyme cascade catalyzed by GOx/HRP_dx@ZIF-8 (x = 23, 17, 15, 13, 11, 10) without CAT or (I) with CAT. (J) Reaction kinetics (number of products, np, versus simulation time) of different radii of enzyme clusters, r = 5, 6, 7, 8, 9, 10, 11(σ) without intermediate decay or (K) with intermediate decay. Reproduced with permission [46]. Copyright 2019, Royal Society of Chemistry.

Fig. 3. (A) Cryo-electron tomography (Cryo-ET) reconstruction and magnified image of a single GOx-aZIF composite. (B) Structure of aZIF by molecular simulations (insets: schemes showing coordination). (C) Density functional theory (DFT) pore size distribution of ZIF-8, amorphous ZIF, and GOx-incorporated amorphous ZIF. (D) X-ray total scattering data and synchrotron radiation X-ray pair distribution function (PDF) of aZIF and ZIF-8. (E) Enzymatic activities of enzyme-ZIF-8 and enzyme-incorporated amorphous ZIFs, including GOx, Candida antarctica lipase B (CALB) and catalase (CAT). Reproduced with permission [52]. Copyright 2019, Springer Nature. (F) Thermal stability of free native HRP and HRP-MOF composites at 60 and 70 °C, respectively. Reproduced with permission [53]. Copyright 2020, American Association for the Advancement of Science.

Fig. 4. (A) Structure of the CALB-Pluronic conjugate with a Pd cluster and principles of DKR of amines catalyzed by CALB and Pd cluster. (B) Structure of the CALB-Pluronic conjugate in benzene. (C) Enzyme activities of Pd/CALB-P hybrid catalyst assayed by ester hydrolysis. (D) Fluorescence spectra of CALB, CALB-P conjugates and xPd/CALB-P hybrid catalysts (x = 0.8, 1.6, 2.2 and 2.5). (E) Free-energy profiles for (S)-1-PEA racemization on pristine Pd(111) and partially oxidized Pd(111) surfaces. (F) Catalytic performance of 0.8Pd/CALB-P at 55 °C and of a combination of commercially available Novozym 435 and Pd/C at 70 and 55 °C for the DKR reactions. (G) Conversions and ee values in ten cycles of the reaction using 0.8Pd/CALB-P as the catalyst. Reproduced with permission [56]. Copyright 2019, Springer Nature.

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Hybrid enzyme catalysts synthesized by a de novo approach for expanding biocatalysis

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