L-Asparaginase from Erwinia carotovora: insights about its stability and activity.
Mol Biol Rep
; 46(1): 1313-1316, 2019 Feb.
Article
em En
| MEDLINE
| ID: mdl-30446961
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 ß-structures in activity. These results provide relevant information to guide formulations with prolonged action in the bloodstream.
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01-internacional
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MEDLINE
Idioma:
En
Ano de publicação:
2019
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Article