Research Article | Volume: 5, Issue: 2, February, 2015

Design, development and characterization of serratiopeptidase loaded albumin nanoparticles

Harpreet Kaur Amit Singh   

Open Access   

Published:  Feb 27, 2015

DOI: 10.7324/JAPS.2015.50215

In recent years, albumin nanoparticles have been widely studied for delivery of various active pharmaceuticals with enhanced accumulation at the site of inflammation. Albumin is a versatile carrier to prepare nanoparticles and nanospheres due to its easy availability in pure form, biodegradability non-toxic and non-immunogenic nature. The mechanism of action of Serratiopeptidase appears to be hydrolysis of histamine, bradykinin and serotonin. Serratiopeptidase also has a proteolytic and fibrinolytic effect. Protein i.e. bovine serum albumin was used to entrap serratiopeptidase enzyme. Protease activity of the enzyme was checked and method was validated to access the active enzyme concentration during formulation. Solvent desolvation method was used for the preparation of BSA nanoparticles. Effect of buffer pH was checked on the enzyme activity. Chloroform was selected and used as solvent for nanoparticle preparation. Effect of various variables such as concentration of BSA, agitation rate, glutarldehyde concentration, time of crosslinking etc. on the formulation was studied. Formed nanoparticles were characterized for drug content, in-vitro release, entrapment efficiency, particle size and size distribution. The formed serratiopeptidase loaded albumin nanoparticles may be used for the treatment of arthritis.

Keyword:     Albumin nanoparticles Serratiopeptidase Solvent desolvation enzyme activity.


Harpreet Kaur, Amit Singh. Design, development and characterization of serratiopeptidase loaded albumin nanoparticles. J App Pharm Sci, 2015; 5 (02): 103-109.

Copyright:The Author(s). This is an open access article distributed under the Creative Commons Attribution Non-Commercial License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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