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PEGylated recombinant L-asparaginase from Erwinia carotovora: Production, properties, and potential applications

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Abstract

N-hydroxysuccinimide ester of monomethoxy polyethylene glycol hemisuccinate was synthesized. It acylated amino groups in a molecule of recombinant L-asparaginase from Erwinia carotovora. A method of L-asparaginase modification by the obtained activated polyethylene glycol derivative was developed. The best results were produced by modification of the enzyme with a 25-fold excess of reagent relative to the enzyme tetramer. The modified L-asparaginase was isolated from the reaction mixture by gel filtration on Sepharose CL-6B. The purified bioconjugate did not contain PEG unbound to the protein, demonstrated high catalytic activity, and exhibited antiproliferative action on cell cultures.

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Correspondence to N. S. Melik-Nubarov.

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Original Russian Text © N.S. Melik-Nubarov, I.D. Grozdova, G.Yu. Lomakina, M.V. Pokrovskaya, V.S. Pokrovski, S.S. Aleksandrova, O.Yu. Abakumova, O.V. Podobed, D.V. Grishin, N.N. Sokolov, 2017, published in Prikladnaya Biokhimiya i Mikrobiologiya, 2017, Vol. 53, No. 2, pp. 164–172.

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Melik-Nubarov, N.S., Grozdova, I.D., Lomakina, G.Y. et al. PEGylated recombinant L-asparaginase from Erwinia carotovora: Production, properties, and potential applications. Appl Biochem Microbiol 53, 165–172 (2017). https://doi.org/10.1134/S0003683817020119

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