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 of the enzyme. The number and enzymatic activity of the cross-linked aggregates strongly depends on the rate of the matrix dissolution: mild dissolution conditions made it possible to increase the number of formed protein particles, the residual specific catalase activity of which is 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. Key words: vaterite, glutaraldehyde, immobilized preparations, intermolecular cross-linking, co-precipitation, CLEAs. Acknowledgment - The authors are grateful to the staff of the M.V. Lomonosov 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 supported in part by Lomonosov Moscow State University (Registration Theme АААА-А21-121011290089-4). The authors also acknowledge Lomonosov Moscow State University Development Program PNR 5.13.

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