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Research Article

Encapsulation of albumin in self-assembled layer-by-layer microcapsules: comparison of co-precipitation and adsorption techniques

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Pages 1302-1310 | Received 02 May 2014, Accepted 09 Jul 2014, Published online: 08 Aug 2014
 

Abstract

Objective: The objective of this study is to prepare and characterize polymeric self-assembled layer-by-layer microcapsules (LbL-MC) to deliver a model protein, bovine serum albumin (BSA). The aim is to compare the BSA encapsulation in LbL-MC using co-precipitation and adsorption methods.

Materials and methods: In co-precipitation method, BSA was co-precipitated with growing calcium carbonate particles to form a core template. Later, poly(styrene sulfonate) and poly(allylamine hydrochloride) were sequentially adsorbed onto the CaCO3 templates. In adsorption method, preformed LbL-MC were incubated with BSA and encapsulation efficiency is optimized for pH and salt concentration. Free and BSA-encapsulated LbL-MC were characterized using Zetasizer, scanning electron microscopy (SEM), Fourier transform infrared spectroscopy and differential scanning calorimeter. Later, in vitro release studies were performed using dialysis membrane method at pH 4, 7.4 and 9.

Results and discussion: Results from Zetasizer and SEM showed free LbL-MC with an average size and zeta-potential of 2.0 ± 0.6 μm and 8.1 ± 1.9 mV, respectively. Zeta-potential of BSA-loaded LbL-MC was (–)7.4 ± 0.7 mV and (–)5.7 ± 1.0 mV for co-precipitation and adsorption methods, respectively. In adsorption method, BSA encapsulation in LbL-MC was found to be greater at pH 6.0 and 0.2 M NaCl. Co-precipitation method provided four-fold greater encapsulation efficiency (%) of BSA in LbL-MC compared with adsorption method. At pH 4, the BSA release from LbL-MC was extended up to 120 h. Polyacrylamide gel electrophoresis showed that BSA encapsulated in LBL-MC through co-precipitation is stable toward trypsin treatment.

Conclusion: In conclusion, co-precipitation method provided greater encapsulation of BSA in LbL-MC. Furthermore, LbL-MC can be developed as carriers for pH-controlled protein delivery.

Acknowledgements

We acknowledge the Department of Chemistry, University of Hyderabad, for SEM analysis.

Declaration of interest

The authors report no declaration of interest.

This work was financially supported by Science and Engineering Research Board-Young Scientist award, (SERB/F/1260/2012-13), Department of Science and Technology, and research initial grant from BITS Pilani, Hyderabad Campus. P. K. M. received CSIR-senior research fellowship for his doctoral studies. Zetasizer was procured from a grant funded by Department of Science and Technology – fund for improvement of infrastructure in science and technology (FIST).

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