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

Authors

  • H.A. Aganyants SPC “Armbiotechnology” NAS RA
  • Ye.A. Hovhannisyan Chair of Biophysics, YSU, Armenia
  • H.O. Koloyan SPC “Armbiotechnology” NAS RA
  • A.S. Hovsepyan SPC “Armbiotechnology” NAS RA
  • A.A. Hambardzumyan SPC “Armbiotechnology” NAS RA

DOI:

https://doi.org/10.46991/PYSUB.2013.47.1.032

Keywords:

$Geobacillus~stearotermophilus$, L-aminoacylase, immobilization, thermal stability, Michaelis constant

Abstract

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

Issue

Vol. 47 No. 1 (230) (2013)

Section

Biology

License

Copyright (c) 2013 Proceedings of the YSU

Creative Commons License

This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.

How to Cite

“IMMOBILIZATION OF RECOMBINANT L-AMINOACYLASE FROM $GEOBACILLUS~STEAROTERMOPHILUS$ AND CHARACTERISTICS OF OBTAINED PREPARATIONS”. 2013. Proceedings of the YSU B: Chemical and Biological Sciences 47 (1 (230): 32-35. https://doi.org/10.46991/PYSUB.2013.47.1.032.