Hajar Ashrafi - Department of pharmaceutics, school of pharmacy, Shiraz university of medical sciences, Shiraz, Iran
amir Azadi - Department of Pharmaceutics, school of Pharmacy, Siraz University of Medical Sciences, Shiraz, Iran
Soliman Mohammadi-Samani - Department of Pharmaceutics, School of Pharmacy, Shiraz University of Medical Sciences, Shiraz, Iran.
Younes Ghasemi - Department of Pharmaceutical Biotechnology, School of Pharmacy and Pharmaceutical Sciences Research Center, Shiraz University of Medical Sciences, Shiraz, Iran
Saeid** Daneshamouz - Department of Pharmaceutics, School of Pharmacy and Pharmaceutical Research Center, Shiraz University of Medical Sciences, Shiraz, Iran

In the present study, the mixing behavior of different groups of surfactants and fatty acid bioconjugated L-asparaginase investigated. The amphiphilic macromolecules were achieved by covalent linkage of fatty acids with different chain lengths (C12, C16, and C22) to the native enzyme, L-asparaginase. The amino group of L-asparaginase lysine residue was conjugated to the carboxylic group of fatty acids, using a carbodiimide activator. The effect of different kinds of surfactants on particle size and enzyme activity of fatty acid bioconjugated L-ASNase was evaluated. The particle sizes of resulted micellar nanocarrier before and after lyophilization and enzyme activity investigated. Among all surfactants, pluronic F-127 with fatty acid bioconjugated L-asparaginase presented more plasma and PBS half-life. Higher activity value after lyophilization for bioconjugate with pluronic F-127 also achieved. These findings from L-asparaginase modification by fatty acid and surfactants indicate a promising stabilized product that may serve as a new candidate for medical purposes.

L-asparaginase, Lipid-protein conjugation, micellar nanocarrier, Pluronic F-127