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Preparation of Catalase Cross-Linked Aggregates Based on Vaterite Matrix

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Abstract

A new technique has been developed for the synthesis of cross-linked catalase aggregates by treatment of the enzyme incorporated into the pores of vaterite microspheres with glutaraldehyde and subsequent dissolving of the inorganic matrix. The resulting aggregates have a spherical shape, a narrow particle size distribution, and a high specific activity. The number and enzyme activity of the cross-linked aggregates strongly depends on the rate of the matrix dissolution: mild conditions of dissolution made it possible to increase the number of formed protein particles, whose residual catalase specific activity was only 2 times less than that of the native enzyme. The storage stability of the cross-linked aggregates is comparable to that of the native enzyme of the same concentration.

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REFERENCES

  1. Brown, G.D., Chemically aggregated enzymes, Methods Enzymol., 1976, vol. 44, pp. 263–280. https://doi.org/10.1016/s0076-6879(76)44022-3

    Article  Google Scholar 

  2. Gupta, M.N., Application of cross-linking techniques to enzyme/protein stabilization and bioconjugate preparation, in Biocatalyst Design for Stability and Specificity, ACS Symp. Ser. Am. Chem. Soc., 1993, pp. 307–324.

    Google Scholar 

  3. Wilson, L., Illanes, A., Soler, L., and Henriquez, M.J., Effect of the degree of cross-linking on the properties of different CLEAs of penicillin acylase, Process Biochem., 2009, vol. 44, pp. 322–326. https://doi.org/10.1016/j.procbio.2008.11.010

    Article  CAS  Google Scholar 

  4. Li, X.D., Wu, J., Jia, D.Ch., et al., Preparation of crosslinked glucoamylase aggregates immobilization by using dextrin and xanthan gum as protecting agents, Catalysts, 2016, vol. 6, no. 6, p. 77. https://doi.org/10.3390/catal6060077

    Article  CAS  Google Scholar 

  5. Guajardo, N., Ahumada, K., de Domınguez, M.P., and Schrebler, R.A., Remarkable stability of Candida antarctica lipase B immobilized via cross-linking aggregates (CLEA) in deep eutectic solvents, Biocatal. Biotransform., 2019, vol. 37, no. 2, pp. 106–114. https://doi.org/10.1080/10242422.2018.1492567

    Article  CAS  Google Scholar 

  6. Wahab, M., Enshasy, H., AbuBakar F., et al., Improvement of cross-linking and stability on cross-linked enzyme aggregate (CLEA)—xylanase by protein surface engineering, Process Biochem., 2019, vol. 86, pp. 40–49. https://www.x-mol.com/paperRedirect/5906292

    Article  Google Scholar 

  7. Illanes, L., Wilson, C., Altamirano, Z., et al., Production of cephalexin in organic medium at high substrateconcentrations with CLEA of penicillin acylase and PGA-450A, Enzyme Microb. Technol., 2007, vol. 40, pp. 195–203. https://doi.org/10.1016/j.enzmictec.2006.03.041

    Article  CAS  Google Scholar 

  8. Primozic, M., Kravanja, G., Knez, Z., et al., Immobilized laccase in the form of (magnetic) cross-linked enzyme aggregates for sustainable diclofenac (bio) degradation, J. Clean. Prod., 2020, vol. 275, article ID 124121. https://doi.org/10.1016/j.jclepro.2020.124121

    Article  CAS  Google Scholar 

  9. Guimaraes, J.R., Miranda, L.P., Fernandez-Lafuente, R., and Tardioli, P.W., Immobilization of Eversa® transform via CLEA technology converts it in a suitable biocatalyst for biolubricant production using waste cooking oil, Molecules, 2021, vol. 26, no. 1, p. 193. https://doi.org/10.3390/molecules26010193

    Article  CAS  Google Scholar 

  10. Schoevaart, R., Wolbers, M.W., Golubovic, M., et al., Preparation, optimization and structures of cross-linked enzyme aggregates (CLEAs), Biotechnol. Bioeng., 2004, vol. 87, pp. 754–762. https://doi.org/10.1002/bit.2018

    Article  CAS  Google Scholar 

  11. Sheldon, R.A., Cross-linked enzyme aggregates (CLEAs): stable and recyclable biocatalysts, Biochem. Soc. Trans., 2007, vol. 35, pp. 1583–1587. https://doi.org/10.1042/BST0351583

    Article  CAS  Google Scholar 

  12. Sheldon, R.A., Cross-linked enzyme aggregates as industrial biocatalysts, Org. Process Res. Dev., 2011, vol. 15, pp. 213–223. https://doi.org/10.1021/op100289f

    Article  CAS  Google Scholar 

  13. Sheldon, R.A., CLEAs, combi-CLEAs and 'smart' magnetic CLEAs: biocatalysis in a bio-based economy, Catalysts, 2019, vol. 9, no. 3, p. 261. https://doi.org/10.3390/catal9030261

    Article  CAS  Google Scholar 

  14. Talecar, S., Joshi, A., Joshi, G., et al., Parameters in preparation and characterization of cross-linked enzyme aggregates (CLEAs), RCS Adv., 2013, vol. 3, pp. 12485–12511. https://doi.org/10.1039/C3RA40818C

    Article  Google Scholar 

  15. Roy, I., Mukherjee, J., and Gupta, M.N., Cross-linked enzyme aggregates for applications in aqueous and nonaqueous media, in Enzyme Stabilization and Immobilization, Minteer, S.D., Ed., Humana Press, 2017, pp. 109–123.

  16. Tai, C.Y. and Chen, F.B., Polymorphism of CaCO3 precipitated in a constant-composition environment, AIChE J., 1998, vol. 44, pp. 1790–1798. https://doi.org/10.1002/aic.690440810

    Article  CAS  Google Scholar 

  17. Volodkin, D.V., Petrov, A.I., Prevot, M., and Sukhorukov, G.B., Matrix polyelectrolyte microcapsules: new system for macromolecule encapsulation, Langmuir, 2004, vol. 20, pp. 3398–3406.

    Article  CAS  Google Scholar 

  18. Feoktistova, N., Rose, J., Prokopovich, V.Z., et al., Controlling the vaterite CaCO3 crystal pores. Design of tailor-made polymer based microcapsules by hard templating, Langmuir, 2016, vol. 32, no. 17, pp. 4229–4238. https://doi.org/10.1021/acs.langmuir.6b00717

    Article  CAS  Google Scholar 

  19. Balabushevich, N.G., Lopez de Guerenu A., Feoktistova N.A., et al. Protein-containing multilayer capsules by templating on mesoporous CaCO3 particles: POST and PRE-loading approaches, Macromol. Biosci., 2015, pp. 2523–2530. https://doi.org/10.1002/mabi.201500243

  20. Binevski, P.V., Balabushevich, N.G., Uvarova, V.I., et al., Biofriendly encapsulation of superoxide dismutase into vaterite CaCO3 crystals. Enzyme activity, release mechanism, and perspectives for ophthalmology, Colloids Surf., 2019, vol. 181, pp. 437–449. https://doi.org/10.1016/j.colsurfb.2019.05.077

    Article  CAS  Google Scholar 

  21. Feoktistova, N.A., Vikulina, A.S., Balabushevich, N.G., et al., Bioactivity of catalase loaded into vaterite CaCO3 crystals via adsorption and co-synthesis, Mater. Des., 2020, vol. 185, article ID 108223. https://doi.org/10.1016/j.matdes.2019.108223

    Article  CAS  Google Scholar 

  22. Lee, Ch.H., Lee, H.S., Lee, J.W., et al., Evaluating enzyme stabilizations in calcium carbonate: comparing in situ and crosslinking mediated immobilization, Int. J. Biol. Macromol., 2021, vol. 175, pp. 341–350. https://doi.org/10.1016/j.ijbiomac.2021.02.028

    Article  CAS  Google Scholar 

  23. Feoktistova, N.G., Stoychev, N., Puretskiy, N., et al., Porous thermo-responsive pNIPAM microgels, Eur. Polym. J., 2015, vol. 68, pp. 650–656. https://doi.org/10.1016/j.eurpolymj.2015.03.040

    Article  CAS  Google Scholar 

  24. Schmidt, S., Behra, M., Uhlig, K., et al., Mesoporous protein particles through colloidal CaCO3 templates, Adv. Funct. Mater., 2013, vol. 23, pp. 116–123. https://doi.org/10.1002/adfm.201201321

    Article  CAS  Google Scholar 

  25. Beers, R.F. and Sizer, I.W., A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase, J. Biol. Chem., 1954, vol. 195, no. 1, pp. 133–140. https://doi.org/10.1016/0009-8981(96)06374-7

    Article  Google Scholar 

  26. Tukel, S.S., Hurrem, F., Yildirim, D., and Alptekin, O., Preparation of crosslinked enzyme aggregates (CLEA) of catalase and its characterization, J. Mol. Cat. B: Enzym., 2013, vol. 97, pp. 252–257. https://doi.org/10.5151/chemeng-cobeq2014-1205-20483-160850

    Article  CAS  Google Scholar 

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ACKNOWLEDGMENTS

The authors are grateful to the staff of Moscow State University A.N. Prusov for help in obtaining TEM images and A.A. Tatarintseva for assistance in obtaining SEM images.

Funding

This work was financially supported by the State Registration Topic AAAA-A21-121011290089-4. The equipment was purchased within the framework of the Moscow State University Development Program.

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Correspondence to N. L. Klyachko.

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The authors declare that they have no conflicts of interest.

This article does not contain any studies involving animals performed by any of the authors.

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Translated by I. Gordon

Abbreviations: Cat, catalase co-precipitated with vaterite after dissolution of the carbonate matrix; Cat–CLEAs, cross-linked catalase aggregates; CC, vaterite microspheres; Cat–GA, catalase co-precipitated with vaterite microspheres and treated with glutaraldehyde after dissolution of the carbonate matrix; CC–Cat, vaterite microspheres co-precipitated with catalase; CC–Cat–GA, vaterite microspheres co-precipitated with catalase and treated with glutaraldehyde; EDTA, ethylenediaminetetraacetic acid; GA, glutaraldehyde; SEM, scanning electron microscopy; TEM, transmission electron microscopy.

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Tagirova, M.A., Eremeev, N.L., Balabushevich, N.G. et al. Preparation of Catalase Cross-Linked Aggregates Based on Vaterite Matrix. Appl Biochem Microbiol 58, 923–931 (2022). https://doi.org/10.1134/S0003683822080075

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