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Natural Science, Biology, 2024, 14, 67–75
DOI: 10.xxxx/example-doi Special Issue 1(2), 2022 186–1928

IMMOBILIZATION OF RECOMBINANT L-AMINOACYLASE FROM GEOBACILLUS STEAROTERMOPHILUS AND CHARACTERISTICS OF OBTAINED PREPARATIONS

Received N/A; revised N/A; accepted N/A
CC BY-NC 4.0 This work is licensed under Creative Commons Attribution–NonCommercial International License (CC BY-NC 4.0).

Thermophilic L-aminoacylase Geobacillus stearotermophiluswas immobilized on silochrome C-80 with glutaraldehyde. Immobilization process does not affect the temperature optima of derived preparations, but increase in the thermal stability of the immobilized aminoacylase was observed. Michaelis constants (Km)were calculated for N-acetyl-L-methionine, N-acetyl-L-valine and N-acetyl-L-alanine. It was shown that as a result of immobilization Km for N-acetyl-L-methionine increased more than 2-fold

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