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. 2019 Feb;46(1):1313-1316.
doi: 10.1007/s11033-018-4459-2. Epub 2018 Nov 16.

L-Asparaginase from Erwinia carotovora: insights about its stability and activity

Marcele Faret  1 , Stephanie Bath de Morais  1 , Nilson Ivo Tonin Zanchin  1 , Tatiana de Arruda Campos Brasil de Souza  2
Affiliations

L-Asparaginase from Erwinia carotovora: insights about its stability and activity

Marcele Faret et al. Mol Biol Rep. 2019 Feb.

Abstract

Enzymatic prospection indicated that L-asparaginase from Erwinia carotovora (ECAR-LANS) posses low glutaminase activity and much effort has been made to produce therapeutic ECAR-LANS. However, its low stability precludes its use in therapy. Herein, biochemical and biophysical assays provided data highlighting the influence of solubilization and storage into ECAR-LANS structure, stability, and activity. Moreover, innovations in recombinant expression and purification guaranteed the purification of functional tetramers. According to solubilization condition, the L-asparaginase activity and temperature of melting ranged up to 25-32%, respectively. CD spectra indicate the tendency of ECAR-LANS to instability and the influence of β-structures in activity. These results provide relevant information to guide formulations with prolonged action in the bloodstream.

Keywords: Biophysical behavior; In solution characterization; L-asparaginase.

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