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Chem Synth 2023;3:5. 10.20517/cs.2022.28 © The Author(s) 2023.
Open Access Research Article

Lysine-modulated synthesis of enzyme-embedded hydrogen-bonded organic frameworks for efficient carbon dioxide fixation

1School of Environmental Science & Engineering, Tianjin University, Tianjin 300072, China.

2Collaborative Innovation Center of Chemical Science and Engineering (Tianjin), Tianjin 300072, China.

3State Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing 10090, China.

4Key Laboratory for Green Chemical Technology of Ministry of Education, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, China.

*Correspondence to: Prof. Jiafu Shi, School of Environmental Science & Engineering, Tianjin University, 92 Weijin Road, Tianjin 300072, China. E-mail: shijiafu@tju.edu.cn ; Prof. Zhongyi Jiang, School of Chemical Engineering & Technology, Tianjin University, 92 Weijin Road, Tianjin 300072, China. E-mail: zhyjiang@tju.edu.cn .

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    Academic Editors: Bao-Lian Su, Damien P. Debecker | Copy Editor: Ke-Cui Yang | Production Editor: Ke-Cui Yang

    © The Author(s) 2023. Open Access This article is licensed under a Creative Commons Attribution 4.0 International License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, sharing, adaptation, distribution and reproduction in any medium or format, for any purpose, even commercially, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.

    Abstract

    Carbonic anhydrase (CA) is an important carbon fixation enzyme. Immobilization of CA can expand its application in the realm of adsorption, catalysis, and so on. As a typical metal-free framework, hydrogen-bonded organic frameworks (HOFs) featuring mild synthesis process, exquisite framework structure and good enzyme compatibility have been used for enzyme embedding. However, the catalytic performance of CA-embedded HOFs (CA@HOFs) is limited by the micropore size of HOFs and the slow adsorption of CO2. Herein, CA@Lys-HOF-1 was synthesized by introducing lysine (Lys), a basic amino acid, during the coprecipitation of CA and HOFs for CO2 fixation. The addition of Lys enlarged the average pore size of HOF-1 from 1.8 to 3.2 nm, whereas the introduced -NH2 groups increased the initial adsorption of CO2 from 0.55 to 1.21 cm3 g-1. Compared to CA@HOF-1, the activity of CA@Lys-HOF-1 was enhanced by 71.25%, and the corresponding production of CaCO3 was enhanced by 12.7%. After eight reaction cycles, CA@Lys-HOF-1 still maintained an output of 9.97 mg of CaCO3 every 5 min, 83.7% of the initial production. It is hoped that the CA@Lys-HOF-1 reported offers a platform for efficient and continuous fixation of CO2.

    INTRODUCTION

    Carbon dioxide (CO2) capture and utilization (CCU) is one of the ever-increasing research topics which can contribute to addressing environmental and ecological issues[1-4]. Enzymes such as formate dehydrogenase (FDH), ribulose-1, 5-bisphosphate carboxylase/oxygenase (RubisCO), and carbonic anhydrase (CA) can accurately activate CO2 to lower the reaction energy barrier, which have received great attention as a green and feasible solution to CCU[5-7]. CA exhibits the highest catalytic rate among all carbon-fixation enzymes, and thus has good potential for the selective transformation of CO2 to HCO3-[8]. However, enzymes that leave the bodies of organisms are easy to inactivate and difficult to reuse[9-11]. One frequently used method to address the above issues is to immobilize enzymes inside carrier materials[12].

    Porous framework materials, such as metal-organic frameworks (MOFs)[13-17], covalent organic frameworks (COFs)[18-22], and hydrogen-bonded organic frameworks (HOFs)[23-25], bearing high specific surface area, high porosity, exquisite framework structure and excellent designability, are emerging carriers for enzyme immobilization. Particularly, HOFs are framework materials linked by hydrogen bonds[26-29], which can be reversibly repaired by simple recrystallization[30,31] and possess better biocompatibility due to the absence of metal ions[32,33]. These advantages make HOFs an excellent candidate as enzyme immobilization carriers[34]. For example, HOF-21 synthesized by Bao et al. can recover its original structure after immersion in aqueous or anionic source solution for 48 h[35]. Tang et al. designed TA-HOFs capable of in situ embedding enzymes with different surface charges and molecular weights[36]. Enzyme in TA-HOFs exhibited remarkably enhanced stability. However, HOFs with micropore size and balanced -NH2/-COOH groups usually showed restricted mass transfer and lower affinity with CO2, therefore exhibiting reduced apparent enzyme activity.

    Herein, HOF-1 composed of two units of Tetrakis(4-amidiniumphenyl)methane and tetrakis (4-carboxyphenyl) methane was selected for CA embedding[37]. The structure of HOF-1 was modulated by introducing basic amino acids during the synthesis process. Briefly, carbonic anhydrase@HOF-1 (CA@HOF-1) was prepared by a coprecipitation method, in which CA was in situ embedded. The structure of CA@HOF-1 was modulated by altering the species and amount of amino acid. We found that basic amino acids, especially lysine (Lys), can interact with the carboxyl monomer of HOF-1 to occupy some of the hydrogen bond formation sites, thus causing defects of HOF-1 to promote mass transfer. Meanwhile, the introduced -NH2 groups also facilitated the initial adsorption of CO2. Compared to CA@HOF-1, CA@Lys-HOF-1 showed a 12.7% enhancement in CO2 fixation efficiency. When CO2 was introduced at a flow rate of 25 mL min-1, CaCO3 precipitation reached 12.26 mg after 5 min of ventilation. After 8 cycles, CA@Lys-HOF-1 maintained an output of 9.97 mg CaCO3 every 5 min. It is believed that Lys-HOF-1 is an ideal framework material for CO2-converting enzyme embedding.

    EXPERIMENTAL

    Materials and chemicals

    Tetrakis(4-amidiniumphenyl)methane tetrahydrochloride (TAM, 95%) was purchased from Jilin Chinese Academy of Sciences-Yanshen Technology Co., Ltd. Tetrakis(4-carboxyphenyl)methane (C29H20O8, 98%) was obtained from Shanghai Macklin Biochemical Technology Co., Ltd. γ-poly-l-glutamic acid (PLGA, 92%), glycine (C2H5NO2, 98%), serine (C3H7NO3, 98%), arginine (C6H14N4O2, 98%), and lysine (C6H14N2O2, 98%) were obtained from Shanghai Aladdin Bio-Chem Technology Co., Ltd. Carbonic anhydrase (EC 4.2.1.1) was acquired from Sigma-Aldrich Co., Ltd. All other chemicals were used as received without any purification.

    Synthesis of HOF-1

    Tetrakis(4-amidiniumphenyl)methane tetrahydrochloride (10 mg) was dissolved in H2O (2.5 mL) to form solution A. Tetrakis(4-carboxyphenyl)methane (7.5 mg) was dispersed in H2O (2375 μL), followed by the addition of aqueous ammonium hydroxide solution (1% v/v, 125 μL) to form solution B. Thereafter, solution B was added to solution A under stirring conditions at room temperature. Precipitation occurred immediately upon mixing. The reaction mixture was left to stir gently in the dark for 1 h. The HOF-1 material was then recovered by centrifugation, washed, dispersed, and centrifuged three times in H2O to remove any unreacted precursors.

    Synthesis of CA@HOF-1

    Tetrakis(4-amidiniumphenyl)methane tetrahydrochloride (10 mg) was dissolved in H2O (1.25 mL) to form solution A. An aqueous solution of CA (1.25 mL of 2 mg mL-1 stock solution) was added to solution A and stirred at room temperature for 10 min to form solution B. Tetrakis(4-carboxyphenyl)methane (7.5 mg) was dissolved in 2375 μL of H2O and 125 μL of 1% NH4OH to form solution C. Solution C was then added dropwise to solution B under stirring. The mixture was then left to stir gently for another 1 h to ensure the completion of the synthesis. Thereafter, CA@HOF-1 was collected by centrifugation and then washed, dispersed, and centrifuged three times in H2O to remove the unreacted precursors and loosely adsorbed CA.

    Synthesis of CA@amino acid-HOF-1

    Tetrakis (4-carboxyphenyl) methane (7.5 mg) was dissolved in 2375 μL of H2O and 125 μL of 1% NH4OH to form solution A. An aqueous solution of CA (0.625 mL of 4 mg mL-1 stock solution) and amino acid (0.625 mL of 1/10/20 mg mL-1 stock solution) was added to solution A and stirred at room temperature for 10 min to form solution B. Tetrakis(4-amidiniumphenyl)methane tetrahydrochloride (10 mg) was dissolved in H2O (1.25 mL) to form solution C. Solution C was then added dropwise to solution B under stirring. The mixture was then left to gently stir for another 1 h to ensure the completion of the synthesis. Thereafter, CA@amino acid-HOF-1 was collected by centrifugation and then washed, dispersed, and centrifuged three times in H2O to remove any unreacted precursors and loosely adsorbed CA.

    Characterization

    The sample morphologies were analyzed by scanning electron microscopy (SEM, S-4800, Hitachi) and transmission electron microscopy (TEM, JEM-100CX II, JEOL). The chemical compositions of the samples were identified by Fourier transform infrared (FTIR) spectrometer (Nicolet-6700, Nicolet). The crystal structures of the samples were identified by X-ray diffraction (XRD, X' Pert Pro), with 2-theta ranging from 10° to 90° by a step width of 0.033° with 15.24° min-1 speed at 40 mA and 40 kV. The specific surface area and pore size distribution of the samples were examined by Brunauer-Emmett-Teller (BET) method based on N2 adsorption/desorption isotherms on an AUTOSORB-1 surface area and pore size analyzer (Quantachrome Instruments).

    Conversion of CO2

    CA@HOF-1 and CA@Lys-HOF-1 were used for the conversion of CO2. In a typical experiment, nitrogen was first injected into the aqueous phase of the reaction device for 10 min to remove CO2 gas in the solution. Then, CO2 with a rate of 25 mL min-1 was injected into the system. A sample was taken every 5 min for follow-up reaction. Specifically, pH value of the reaction solution was detected by a pH meter and kept at 7.9, which was adjusted by adding 5 mol L-1 NaOH. Then, a certain amount of reaction solution was mixed with 670 mmol L-1 calcium chloride solution. The mixture was shaken at 200 r min-1 to form CaCO3 precipitate. The precipitated CaCO3 was filtered by a filter paper with an average pore diameter of 2.5 μm, which was then dried overnight and weighed to determine the relative yield of CaCO3.

    RESULTS AND DISCUSSION

    Preparation and Characterization of CA@HOF-1 and CA@Lys-HOF-1

    A reported HOF material (HOF-1) was chosen for the embedding of CA[37]. The preparation and structure regulation of CA@HOF-1 are shown in Figure 1. Briefly, HOF-1 was prepared by mixing tetrakis(4-amidiniumphenyl)methane tetrahydrochloride (monomer 1) solution and tetrakis(4-carboxyphenyl)methane (monomer 2) solution under stirring at room temperature [Supplementary Figure 1]. CA@Lys-HOF-1 was prepared by introducing CA and lysine (Lys) during the HOF-1 synthesis process. For control, CA@HOF-1 was also prepared by only adding CA in the HOF-1 synthesis. In advance of the discussion about CA@HOF-1 and CA@Lys-HOF-1, the chemical composition and physical structure of HOF-1 were characterized by FTIR, XRD and 13C-NMR, which are shown in Supplementary Figures 2 and 3.

    Figure 1. Schematic showing the preparation process of CA@HOF-1 and CA@Lys-HOF-1.

    The topological structures of all samples were also examined by SEM and TEM. As shown in Figure 2 and Supplementary Figure 4, both CA@HOF-1 and CA@Lys-HOF-1 maintain the rod-like structure of HOF-1 with similar dimensions (around 300 nm wide). This indicates that the incorporation of CA and Lys did not alter the structure and size of HOF-1 during crystallization. As depicted in Figure 2C, some defects can be observed on the surface of CA@Lys-HOF-1, while CA@HOF-1 and HOF-1 remain intact. Figure 2D further shows that CA@HOF-1 and CA@Lys-HOF-1 well maintain the crystal structure of HOF-1 with the characteristic peaks at 2θ values of 8.6°, and 17.4°. The results of FTIR analysis of CA@HOF-1 and CA@Lys-HOF-1 are shown in Figure 2E. The absorption band centered at around 1030 cm-1 may be assigned to the N-H bending vibration of amide in Lys, indicating the introduction of Lys into HOF-1. To reveal the variation of surface area and pore size distribution of HOF-1 after modulation and enzyme embedding, the N2 adsorption-desorption isotherms of HOF-1, CA@HOF-1, and CA@Lys-HOF-1 were examined [Supplementary Figure 5]. As shown in Figure 2F and Table 1, CA@Lys-HOF-1 shows a larger pore size and broader size distribution, which may facilitate the transfer of CO2 from the particle surface to CA. CA@Lys-HOF-1 also has a larger surface area due to the defects caused by Lys, which provides more sites for CO2 conversion. Then, the CO2 adsorption tests were performed and the results are shown in Figure 2G and Supplementary Figure 6. The CO2 adsorption of CA@Lys-HOF-1 is higher when the CO2 partial pressure is low, a result due to the relatively larger pore size. With an increase in CO2 partial pressure, CA@Lys-HOF-1 reaches CO2 adsorption saturation most quickly, mainly owing to the higher amount of -NH2 with high CO2 affinity on the particle surface. As the pressure continued to increase, the final amount of CO2 adsorption of CA@Lys-HOF-1 was close to that of HOF-1 and CA@HOF-1.

    Figure 2. TEM images of (A) HOF-1; (B) CA@HOF-1; and (C) CA@Lys-HOF-1; (D) XRD patterns; (E) FTIR spectra; (F) pore size distribution; and (G) CO2 adsorption capacity of HOF-1, CA@HOF-1, and CA@Lys-HOF-1.

    Table 1

    BET analysis and initial CO2 adsorption volume of HOF-1, CA@HOF-1, and CA@Lys-HOF-1

    HOF-1CA@HOF-1CA-Lys@HOF-1
    Surface area (m2 g-1)13.114.919.7
    Main pore diameter (nm)1.83.03.2
    Initial CO2 adsorption volume (cm3 g-1)-0.0250.5461.214

    Subsequently, EDS mapping was performed to further investigate whether enzymes were embedded in HOF-1. As shown in Figure 3, the distribution of C and N (the main elements in the two monomers of HOF-1) match the morphology of materials, which can also prove the successful synthesis of HOF-1. Particularly, S (the characteristic element of CA) is uniformly dispersed in the two samples of CA@HOF-1 and CA@Lys-HOF-1, indicating the successful embedding of CA.

    Figure 3. Bright-field images (left) and EDS elemental mapping (right) of C, N, and S for (A) HOF-1; (B) CA@HOF-1; and (C) CA@Lys-HOF-1.

    Catalytic activity of CA@Lys-HOF-1

    In this work, five different types of (poly) amino acids [Supplementary Figure 7] were adopted to regulate the structure and catalytic performance of CA@HOF-1. Specifically, the hydrogen bonds in HOF-1 are formed between -NH2 and -COOH of the two monomers, while amino acids are organic compounds containing both -NH2 and -COOH in the molecule. Amino acids may occupy part of the hydrogen bond formation site, and interfere with the synthesis of HOF-1 through competitive ligand interaction, thus altering the pore size of HOF-1 and influencing the mass transfer.

    When γ-poly-l-glutamic acid (PLGA) was introduced, its -COOH groups can rapidly bind to monomer 1, inhibiting the formation of HOF-1. [Supplementary Figure 8]. This was probably due to the preferential combination of -COOH in PLGA and -NH2 in monomer. Among the other four types of amino acid-modulated CA@HOF-1, the CA@Lys-HOF-1 exerted the highest activity [Supplementary Figures 9 and 10].

    The catalytic activity of HOF-1, Lys-HOF-1, CA@HOF-1, and CA@Lys-HOF-1 were tested by dispersing them individually in solution for CO2 conversion. The activity was reflected by detecting the pH change in the solution after the ventilation of CO2. The solution without catalyst samples was chosen as control, the ΔpH was measured in real-time, and the value at the highest point was chosen to reflect the catalyst activity. Figure 4A and B shows that the activity of CA@Lys-HOF-1 was enhanced. The higher activity of CA@Lys-HOF-1 may be attributed to the defects resulting from Lys, which promoted mass transfer. The -NH2 groups in Lys were also introduced into the material, which fortified the affinity between the materials and CO2 [Supplementary Figure 11]. Furthermore, we investigated the effect of Lys concentrations on the activity. As seen in Figure 4C and D, moderate concentration of Lys is favorable for HOF-1 modulation, thus acquiring the most active CA@Lys-HOF-1. It should be noted that the results of Arg modulation are shown in Supplementary Figure 12, which also shows the same result.

    Figure 4. (A and B) Catalytic activity of HOF-1, Lys-HOF-1, CA@HOF-1, CA@Lys-HOF-1, and Free CA; (C and D) Catalytic activity of CA@HOF-1 modulated by different concentrations of Lys.

    Stability and CO2 fixation ability of CA@Lys-HOF-1

    Subsequently, the stability, reusability, and CO2 fixation ability of CA@Lys-HOF-1 were investigated. As shown in Figure 5, Lys-HOF-1 exhibits better protection of CA at different pH values. Regarding the thermal stability, the protective ability of Lys-HOF-1 for CA began to decrease when the temperature was higher than 60 °C. This may be owing to the weakened strength of hydrogen bonds within the carrier material after Lys modification, which made Lys-HOF-1 more prone to decomposition at higher temperatures. The reusability of CA@Lys-HOF-1 was also evaluated for its importance in industrial applications. As shown in Figure 5C, CA@Lys-HOF-1 shows excellent recyclability. After the 8th cycle of reaction, CA@Lys-HOF-1 still maintained 83.7% of its initial activity, and demonstrated unaltered morphological and crystal structure [Supplementary Figure 13].

    Figure 5. (A) pH stability; (B) thermal stability; (C) reusability; and (D) production of CaCO3 enabled by CA@Lys-HOF-1.

    Finally, to examine the CO2 fixation ability of CA@Lys-HOF-1, CO2 was introduced at a flow rate of 25 mL min–1, and the CaCO3 mineralization reaction was performed after 5 min of ventilation. In detail, the reaction rates of the four samples, including HOF-1, Lys-HOF-1, CA@HOF-1, and CA@ Lys-HOF-1, were assessed by measuring the amount of CaCO3 precipitate produced. As shown in Figure 5D, the CaCO3 precipitate amount of HOF-1, Lys-HOF-1, CA@HOF-1, and CA@Lys-HOF-1 is, respectively, 4.81 mg, 6.29 mg, 10.88 mg, 12.26 mg. The production of CaCO3 enabled by CA@Lys-HOF-1 was the highest, again validating the superiority of CA@Lys-HOF-1 in fortifying CO2 fixation processes. Moreover, a hot filtration[38] experiment was performed over CA@Lys-HOF-1 for CO2 mineralization. As shown in Supplementary Figure 14, no more increment in the production of CaCO3 is observed after the filtration process, suggesting the heterogeneous nature of our catalytic system.

    CONCLUSIONS

    In summary, HOF-1 modulated by amino acids was synthesized through a coprecipitation method for CA immobilization. By regulating the type and concentration of introduced amino acids, CA@Lys-HOF-1 with optimized activity and desirable stability was obtained. Compared with unmodulated CA@HOF-1, the activity of CA@Lys-HOF-1 was enhanced by 71.3%, whereas the CO2 fixation efficiency reflected by CaCO3 production was enhanced by 12.7%. This could be ascribed to the large pore size of CA@Lys-HOF-1 that facilitated CO2 transfer as well as the abundant surface -NH2 groups that promoted CO2 adsorption. Moreover, CA@Lys-HOF-1 maintained over 80% of the initial activity after the 8th cycle reaction. Our findings may pave the way for the immobilization of CA and other CO2-fixation enzymes.

    DECLARATIONS

    Authors’ contributions

    Carried out the catalyst preparation, characterization, and catalytic tests, and prepared the draft manuscript: Zhang B

    Performed part of the catalyst characterization: Chu Z, Zhang J, Wu Z

    Performed the TEM characterization: Yang D, Wu H

    Planned the study, analyzed the data and wrote the manuscript: Shi J, Jiang Z

    Availability of data and materials

    Not applicable.

    Financial support and sponsorship

    This work was supported by the National Key R&D Program of China (2022YFC2105902), the National Key R&D Program of China (2021YFC2102300), the National Natural Science Funds of China (22122809), Open Funding Project of the State Key Laboratory of Biochemical Engineering (2020KF-06), and Tianjin Synthetic Biotechnology Innovation Capacity Improvement Project (TSBICIP-KJGG-003) for financial support.

    Conflicts of interest

    All authors declared that there are no conflicts of interest.

    Ethical approval and consent to participate

    Not applicable.

    Consent for publication

    Not applicable.

    Copyright

    © The Author(s) 2023.

    Supplementary Materials

    References

    • 1. Yaashikaa P, Senthil Kumar P, Varjani SJ, Saravanan A. A review on photochemical, biochemical and electrochemical transformation of CO2 into value-added products. J CO2 Util 2019;33:131-47.

      DOI
    • 2. Zhao T, Feng G, Chen W, et al. Artificial bioconversion of carbon dioxide. Chinese J Catal 2019;40:1421-37.

      DOIPubMed
    • 3. Markewitz P, Kuckshinrichs W, Leitner W, et al. Worldwide innovations in the development of carbon capture technologies and the utilization of CO2. Energy Environ Sci 2012;5:7281.

      DOI
    • 4. Hermida-Carrera C, Kapralov MV, Galmés J. Rubisco catalytic properties and temperature response in crops. Plant Physiol 2016;171:2549-61.

      DOIPubMed PMC
    • 5. Cummins PL, Kannappan B, Gready JE. Directions for optimization of photosynthetic carbon fixation: RuBisCo’s efficiency may not be so constrained after all. Front Plant Sci 2018;9:183.

      DOIPubMed PMC
    • 6. Itakura AK, Chan KX, Atkinson N, et al. A Rubisco-binding protein is required for normal pyrenoid number and starch sheath morphology in Chlamydomonas reinhardtii. Proc Natl Acad Sci USA 2019;116:18445-54.

      DOIPubMed PMC
    • 7. Valegård K, Andralojc PJ, Haslam RP, et al. Structural and functional analyses of Rubisco from arctic diatom species reveal unusual posttranslational modifications. J Biol Chem 2018;293:13033-43.

      DOIPubMed PMC
    • 8. Lindskog S, Coleman JE. The catalytic mechanism of carbonic anhydrase. Proc Natl Acad Sci USA 1973;70:2505-8.

      DOI
    • 9. Cao S, Yue D, Li X, et al. Novel nano-/micro-biocatalyst: soybean epoxide hydrolase immobilized on UiO-66-NH2 MOF for efficient biosynthesis of enantiopure (R)-1, 2-octanediol in deep eutectic solvents. ACS Sustain Chem Eng 2016;4:3586-95.

      DOI
    • 10. Cao S, Xu P, Ma Y, et al. Recent advances in immobilized enzymes on nanocarriers. Chinese J Catal 2016;37:1814-23.

      DOI
    • 11. Cao S, Xu H, Lai L, et al. Magnetic ZIF-8/cellulose/Fe3O4 nanocomposite: preparation, characterization, and enzyme immobilization. Bioresour Bioprocess 2017;4:1-7.

      DOI
    • 12. Alizadeh N, Salimi A, Hallaj R, Fathi F, Soleimani F. Ni-hemin metal-organic framework with highly efficient peroxidase catalytic activity: toward colorimetric cancer cell detection and targeted therapeutics. J Nanobiotechnology 2018;16:93.

      DOIPubMed PMC
    • 13. Drout RJ, Robison L, Farha OK. Catalytic applications of enzymes encapsulated in metal-organic frameworks. Coord Chem Rev 2019;381:151-60.

      DOI
    • 14. Wu X, Hou M, Ge J. Metal-organic frameworks and inorganic nanoflowers: a type of emerging inorganic crystal nanocarrier for enzyme immobilization. Catal Sci Technol 2015;5:5077-85.

      DOI
    • 15. Doonan C, Riccò R, Liang K, Bradshaw D, Falcaro P. Metal-organic frameworks at the biointerface: synthetic strategies and applications. Acc Chem Res 2017;50:1423-32.

      DOIPubMed
    • 16. Riccò R, Liang W, Li S, et al. Metal-organic frameworks for cell and virus biology: a perspective. ACS Nano 2018;12:13-23.

      DOIPubMed
    • 17. Du Y, Gao J, Zhou L, et al. MOF-based nanotubes to hollow nanospheres through protein-induced soft-templating pathways. Adv Sci (Weinh) 2019;6:1801684.

      DOIPubMed PMC
    • 18. Sun Q, Fu CW, Aguila B, et al. Pore environment control and enhanced performance of enzymes infiltrated in covalent organic frameworks. J Am Chem Soc 2018;140:984-92.

      DOIPubMed
    • 19. Serre C, Kitagawa S, Dietzel PD. Introduction to special issue: metal organic frameworks. Microporous Mesoporous Mater 2012;157:1-2.

      DOI
    • 20. Furukawa H, Cordova KE, O'Keeffe M, Yaghi OM. The chemistry and applications of metal-organic frameworks. Science 2013;341:1230444.

      DOI
    • 21. Eum K, Jayachandrababu KC, Rashidi F, et al. Highly tunable molecular sieving and adsorption properties of mixed-linker zeolitic imidazolate frameworks. J Am Chem Soc 2015;137:4191-7.

      DOIPubMed
    • 22. Zhang H, Hou J, Hu Y, et al. Ultrafast selective transport of alkali metal ions in metal organic frameworks with subnanometer pores. Sci Adv 2018;4:eaaq0066.

      DOIPubMed PMC
    • 23. Luo J, Wang J, Zhang J, Lai S, Zhong D. Hydrogen-bonded organic frameworks: design, structures and potential applications. CrystEngComm 2018;20:5884-98.

      DOI
    • 24. Lin RB, He Y, Li P, Wang H, Zhou W, Chen B. Multifunctional porous hydrogen-bonded organic framework materials. Chem Soc Rev 2019;48:1362-89.

      DOIPubMed
    • 25. Hisaki I, Xin C, Takahashi K, Nakamura T. Designing hydrogen-bonded organic frameworks (HOFs) with permanent porosity. Angew Chem Int Ed Engl 2019;58:11160-70.

      DOIPubMed
    • 26. Luzuriaga MA, Benjamin CE, Gaertner MW, et al. ZIF-8 degrades in cell media, serum, and some-but not all-common laboratory buffers. Supramol Chem 2019;31:485-90.

      DOI
    • 27. Velásquez-hernández MDJ, Ricco R, Carraro F, et al. Degradation of ZIF-8 in phosphate buffered saline media. CrystEngComm 2019;21:4538-44.

      DOI
    • 28. Luzuriaga MA, Welch RP, Dharmarwardana M, et al. Enhanced Stability and controlled delivery of MOF-encapsulated vaccines and their immunogenic response in vivo. ACS Appl Mater Interf 2019;11:9740-6.

      DOIPubMed
    • 29. Sun CY, Qin C, Wang XL, et al. Zeolitic Imidazolate framework-8 as efficient pH-sensitive drug delivery vehicle. Dalton Trans 2012;41:6906-9.

      DOIPubMed
    • 30. Persico F, Wuest JD. Use of hydrogen bonds to control molecular aggregation. Behavior of a self-complementary dipyridone designed to self-replicate. J Org Chem 1993;58:95-9.

      DOI
    • 31. Russell VA, Evans CC, Li W, Ward MD. Nanoporous molecular sandwiches: pillared two-dimensional hydrogen-bonded networks with adjustable porosity. Science 1997;276:575-9.

      DOIPubMed
    • 32. Tamames-Tabar C, Cunha D, Imbuluzqueta E, et al. Cytotoxicity of nanoscaled metal-organic frameworks. J Mater Chem B 2014;2:262-71.

      DOIPubMed
    • 33. Grall R, Hidalgo T, Delic J, Garcia-Marquez A, Chevillard S, Horcajada P. In vitro biocompatibility of mesoporous metal (III; Fe, Al, Cr) trimesate MOF nanocarriers. J Mater Chem B 2015;3:8279-92.

      DOIPubMed
    • 34. Tang Z, Li X, Tong L, et al. A biocatalytic cascade in an ultrastable mesoporous hydrogen-bonded organic framework for point-of-care biosensing. Angew Chem Int Ed Engl 2021;60:23608-13.

      DOIPubMed
    • 35. Bao Z, Xie D, Chang G, et al. Fine tuning and specific binding sites with a porous hydrogen-bonded metal-complex framework for gas selective separations. J Am Chem Soc 2018;140:4596-603.

      DOIPubMed
    • 36. Tang J, Liu J, Zheng Q, et al. In-situ encapsulation of protein into nanoscale hydrogen-bonded organic frameworks for intracellular biocatalysis. Angew Chem Int Ed Engl 2021;60:22315-21.

      DOIPubMed
    • 37. Liang W, Carraro F, Solomon MB, et al. Enzyme encapsulation in a porous hydrogen-bonded organic framework. J Am Chem Soc 2019;141:14298-305.

      DOIPubMed
    • 38. Qin Z, Li H, Yang X, Chen L, Li Y, Shen K. Heterogenizing homogeneous cocatalysts by well-designed hollow MOF-based nanoreactors for efficient and size-selective CO2 fixation. Appl Catal B Environ 2022;307:121163.

      DOI

    Cite This Article

    OAE Style

    Zhang B, Shi J, Chu Z, Zhang J, Wu Z, Yang D, Wu H, Jiang Z. Lysine-modulated synthesis of enzyme-embedded hydrogen-bonded organic frameworks for efficient carbon dioxide fixation. Chem Synth 2023;3:5. http://dx.doi.org/10.20517/cs.2022.28

    AMA Style

    Zhang B, Shi J, Chu Z, Zhang J, Wu Z, Yang D, Wu H, Jiang Z. Lysine-modulated synthesis of enzyme-embedded hydrogen-bonded organic frameworks for efficient carbon dioxide fixation. Chemical Synthesis. 2023; 3(1):5. http://dx.doi.org/10.20517/cs.2022.28

    Chicago/Turabian Style

    Zhang, Boyu, Jiafu Shi, Ziyi Chu, Jiaxu Zhang, Zhenhua Wu, Dong Yang, Hong Wu, Zhongyi Jiang. 2023. "Lysine-modulated synthesis of enzyme-embedded hydrogen-bonded organic frameworks for efficient carbon dioxide fixation" Chemical Synthesis. 3, no.1: 5. http://dx.doi.org/10.20517/cs.2022.28

    ACS Style

    Zhang, B.; Shi J.; Chu Z.; Zhang J.; Wu Z.; Yang D.; Wu H.; Jiang Z. Lysine-modulated synthesis of enzyme-embedded hydrogen-bonded organic frameworks for efficient carbon dioxide fixation. Chem. Synth. 20233, 5. http://dx.doi.org/10.20517/cs.2022.28

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    Author Biographies

    • Boyu Zhang
      Boyu Zhang received his BS and MS degrees under the tutelage of Professor Jiafu Shi at the School of Environmental Science and Engineering at Tianjin University in 2020 and 2023, respectively. He will pursue a Ph.D. under the tutelage of Professor Jiafu Shi. His research interests include enzyme catalysis and CO2 conversion.
      Boyu Zhang
      Boyu Zhang received his BS and MS degrees under the tutelage of Professor Jiafu Shi at the School of Environmental Science and Engineering at Tianjin University in 2020 and 2023, respectively. He will pursue a Ph.D. under the tutelage of Professor Jiafu Shi. His research interests include enzyme catalysis and CO2 conversion.
    • Jiafu Shi
      Jiafu Shi is a Professor at the School of Environmental Science and Engineering at Tianjin University. He obtained his Ph.D. from Tianjin University in 2013. He was a visiting scholar at the University of California at Berkeley with Professor Phillip B. Messersmith from 2016 to 2017. He is the winner of the National Science Fund for Excellent Young Scholars in China. His research interest includes enzyme-catalyzed biomanufacturing processes. He has co-authored over 100 peer-reviewed papers, including Chemical Society Reviews, Journal of the American Chemical Society, ACS Catalysis, Advanced Functional Materials, Chem, Angewandte Chemie International Edition, Joule, etc.
      Jiafu Shi
      Jiafu Shi is a Professor at the School of Environmental Science and Engineering at Tianjin University. He obtained his Ph.D. from Tianjin University in 2013. He was a visiting scholar at the University of California at Berkeley with Professor Phillip B. Messersmith from 2016 to 2017. He is the winner of the National Science Fund for Excellent Young Scholars in China. His research interest includes enzyme-catalyzed biomanufacturing processes. He has co-authored over 100 peer-reviewed papers, including Chemical Society Reviews, Journal of the American Chemical Society, ACS Catalysis, Advanced Functional Materials, Chem, Angewandte Chemie International Edition, Joule, etc.
    • Ziyi Chu
      Ziyi Chu received her BS degree from the School of Environmental Science and Technology at Tianjin University in 2021. She is currently pursuing her MS degree under the tutelage of Professor Jiafu Shi. Her research interests include enzyme catalysis and functional sugar synthesis.
      Ziyi Chu
      Ziyi Chu received her BS degree from the School of Environmental Science and Technology at Tianjin University in 2021. She is currently pursuing her MS degree under the tutelage of Professor Jiafu Shi. Her research interests include enzyme catalysis and functional sugar synthesis.
    • Jiaxu Zhang
      Jiaxu Zhang received her BS degree from the School of Chemistry and Environmental Science at Hebei University in 2020. She received her MS degree under the tutelage of Professor Jiafu Shi at the School of Environmental Science and Engineering at Tianjin University in 2023. Her research interests include enzyme catalysis and functional sugar synthesis.
      Jiaxu Zhang
      Jiaxu Zhang received her BS degree from the School of Chemistry and Environmental Science at Hebei University in 2020. She received her MS degree under the tutelage of Professor Jiafu Shi at the School of Environmental Science and Engineering at Tianjin University in 2023. Her research interests include enzyme catalysis and functional sugar synthesis.
    • Zhenhua Wu
      Zhenhua Wu received his BS degree from College of Chemical Engineering and Technology at Nanjing Tech University in 2018 and his MS degree from the School of Chemical Engineering and Technology at Tianjin University in 2021. He is currently pursuing his Ph.D. under the tutelage of Professor Jiafu Shi. His research interests include biocatalysis and nanostructured biohybrid materials.
      Zhenhua Wu
      Zhenhua Wu received his BS degree from College of Chemical Engineering and Technology at Nanjing Tech University in 2018 and his MS degree from the School of Chemical Engineering and Technology at Tianjin University in 2021. He is currently pursuing his Ph.D. under the tutelage of Professor Jiafu Shi. His research interests include biocatalysis and nanostructured biohybrid materials.
    • Dong Yang
      Dong Yang is an Associate Professor at the School of Chemical Engineering and Technology of Tianjin University. He obtained his Ph.D. at Northeast Forestry University in 2001 under the guidance of Professor Lijia An. After a stint with Professor Limin Qi as a Postdoctoral at Peking University, he joined the faculty of Tianjin University in 2004. His research interests encompass functional nanomaterials, biocatalysis and photocatalysis. He has co‐authored over 120 peer‐reviewed papers, including Advanced Materials, ACS Nano, ACS Catalysis, ACS Sustainable Chemistry & Engineering, ACS Applied Materials & Interfaces, etc.
      Dong Yang
      Dong Yang is an Associate Professor at the School of Chemical Engineering and Technology of Tianjin University. He obtained his Ph.D. at Northeast Forestry University in 2001 under the guidance of Professor Lijia An. After a stint with Professor Limin Qi as a Postdoctoral at Peking University, he joined the faculty of Tianjin University in 2004. His research interests encompass functional nanomaterials, biocatalysis and photocatalysis. He has co‐authored over 120 peer‐reviewed papers, including Advanced Materials, ACS Nano, ACS Catalysis, ACS Sustainable Chemistry & Engineering, ACS Applied Materials & Interfaces, etc.
    • Hong Wu
      Hong Wu is a Professor at the School of Chemical Engineering and Technology at Tianjin University. She received her Ph.D. from Tianjin University. Her research interests include membranes and membrane processes, enzyme catalysis, etc. She has co-authored over 300 peer-reviewed papers including Nature Communications, Chemical Society Reviews, Journal of the American Chemical Society, Angewandte Chemie International Edition, Advanced Materials, Advanced Functional Materials, etc.
      Hong Wu
      Hong Wu is a Professor at the School of Chemical Engineering and Technology at Tianjin University. She received her Ph.D. from Tianjin University. Her research interests include membranes and membrane processes, enzyme catalysis, etc. She has co-authored over 300 peer-reviewed papers including Nature Communications, Chemical Society Reviews, Journal of the American Chemical Society, Angewandte Chemie International Edition, Advanced Materials, Advanced Functional Materials, etc.
    • Zhongyi Jiang
      Zhongyi Jiang is a Professor at the School of Chemical Engineering and Technology at Tianjin University. He obtained his Ph.D. from Tianjin University in 1994. He was a visiting scholar at the University of Minnesota with Prof. Edward Cussler in 1997 and California Institute of Technology with Prof. David Tirrell in 2009. He is the winner of the National Science Fund for Distinguished Young Scholars in China, a Cheung Kong Chair Professor, Fellow of the Royal Society of Chemistry. His research interests include biomimetic and bioinspired membranes and membrane processes, biocatalysis, and photocatalysis. He has co‐authored over 600 peer‐reviewed papers, including Nature Sustainability, Nature Communications, Chemical Society Reviews, Journal of the American Chemical Society, Angewandte Chemie International Edition, Advanced Materials, Advanced Functional Materials, ACS Catalysis, etc.
      Zhongyi Jiang
      Zhongyi Jiang is a Professor at the School of Chemical Engineering and Technology at Tianjin University. He obtained his Ph.D. from Tianjin University in 1994. He was a visiting scholar at the University of Minnesota with Prof. Edward Cussler in 1997 and California Institute of Technology with Prof. David Tirrell in 2009. He is the winner of the National Science Fund for Distinguished Young Scholars in China, a Cheung Kong Chair Professor, Fellow of the Royal Society of Chemistry. His research interests include biomimetic and bioinspired membranes and membrane processes, biocatalysis, and photocatalysis. He has co‐authored over 600 peer‐reviewed papers, including Nature Sustainability, Nature Communications, Chemical Society Reviews, Journal of the American Chemical Society, Angewandte Chemie International Edition, Advanced Materials, Advanced Functional Materials, ACS Catalysis, etc.

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