IMMOBILIZATION OF RECOMBINANT L-AMINOACYLASE FROM $GEOBACILLUS~STEAROTERMOPHILUS$ AND CHARACTERISTICS OF OBTAINED PREPARATIONS
DOI:
https://doi.org/10.46991/PYSU:B/2013.47.1.032Keywords:
$Geobacillus~stearotermophilus$, L-aminoacylase, immobilization, thermal stability, Michaelis constantAbstract
Thermophilic L-aminoacylase Geobacillus stearotermophilus was 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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Published
2013-03-10
How to Cite
Aganyants, H.A., Ye.A. Hovhannisyan, H.O. Koloyan, A.S. Hovsepyan, and A.A. Hambardzumyan. 2013. “IMMOBILIZATION OF RECOMBINANT L-AMINOACYLASE FROM $GEOBACILLUS~STEAROTERMOPHILUS$ AND CHARACTERISTICS OF OBTAINED PREPARATIONS”. Proceedings of the YSU B: Chemical and Biological Sciences 47 (1 (230):32-35. https://doi.org/10.46991/PYSU:B/2013.47.1.032.
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Biology
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