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.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Asparaginase
/
Pectobacterium carotovorum
Idioma:
En
Revista:
Mol Biol Rep
Ano de publicação:
2019
Tipo de documento:
Article
País de afiliação:
Brasil