Influence of post-emulsification drying processes on the microencapsulation of Human Serum Albumin

In the present work, methods used to microencapsulate Human Serum Albumin (HSA) in a biodegradable polymer were compared for their effects on the physicochemical characteristics of HSA-loaded microparticles and on the release and integrity of encapsulated HSA. The polymer used was poly(d,l-lactide-co-glycolide) (75:25) (PLGA) (Boehringer Ingelheim, Resomer RG 752, MW 20,900). Microparticles were formulated by (i) w/o/w emulsification and freeze-drying (EFD) or (ii) w/o/w emulsification and spray-drying (ESD). Particle morphology and size were evaluated by scanning electron microscopy and by laser diffraction analysis. Loading, encapsulation efficiency and protein release were determined using a commercial protein assay kit. Protein integrity was evaluated by sodium dodecyl sulphate–polyacrylamide gel electrophoresis (SDS–PAGE) analysis. Particles produced by emulsification/spray-drying exhibited greater diversity in shape than those produced by emulsification/freeze-drying. Additionally, protein loading values were significantly higher for particles produced by emulsification/spray-drying rather than particles produced by emulsification/freeze-drying. The structural integrity of encapsulated protein was confirmed for particles produced by both processes. The fraction of HSA released was similar for both formulations. The emulsification/spray-drying technique described appears to be a rapid and efficient method for the preparation of PLGA microparticles loaded with a model protein.