Immobilization of L-asparaginase on Oxidized Bacterial Cellulose to Improve the Thermal Stability of the Enzyme

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Published: Oct 1, 2024
DOI: https://doi.org/10.18097/BMCRM00234
Keywords:
L-asparaginase; bacterial cellulose; immobilization; thermal stability

Main Article Content

A.N. Shishparenok
Institute of Biomedical Chemistry, 10 Pogodinskaya str., Moscow, 119121 Russia
S.A. Koroleva
Patrice Lumumba Peoples` Friendship University of Russia (RUDN University), 6 Miklukho-Maklaya str., Moscow, 117198 Russia
I.D. Zlotnikov
Moscow State University, 1 Leninskie Gory str., Moscow, 119192 Russia
Yu.A. Gladilina
Institute of Biomedical Chemistry, 10 Pogodinskaya str., Moscow, 119121 Russia
M.V. Pokrovskaya
Institute of Biomedical Chemistry, 10 Pogodinskaya str., Moscow, 119121 Russia
S.S. Alexandrova
Institute of Biomedical Chemistry, 10 Pogodinskaya str., Moscow, 119121 Russia
D.D. Zhdanov
Institute of Biomedical Chemistry, 10 Pogodinskaya str., Moscow, 119121 Russia

Abstract

Bacterial cellulose (BC) membranes can be modified for covalent immobilization of macromolecules. One type of modification is oxidation, after which the oxidized BC membrane (OBC) could be used as a matrix for covalent immobilization of enzymes. In this work, the BC membrane was chemically oxidized with sodium periodate (NaIO4) to increase the stability of immobilized mesophilic L-asparaginase (L-ASNase) from Erwinia carotovora (EwA). IR spectroscopy confirmed the immobilization of L-ASNase EwA on OBC membranes. Immobilization of the enzyme increased its temperature optimum for its activity by 15°C and raised the inactivation temperature to 60°C. The OBC membrane could be used as a potential carrier for covalent immobilization of enzymes to improve their pharmacological properties by increasing their thermostability.

Article Details

How to Cite
Shishparenok, A., Koroleva, S., Zlotnikov, I., Gladilina, Y., Pokrovskaya, M., Alexandrova, S., & Zhdanov, D. (2024). Immobilization of L-asparaginase on Oxidized Bacterial Cellulose to Improve the Thermal Stability of the Enzyme. Biomedical Chemistry: Research and Methods, 7(3), e00234. https://doi.org/10.18097/BMCRM00234
Issue
Vol. 7 No. 3 (2024)
Section
EXPERIMENTAL RESEARCH

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