This paper describes formulation of a model protein, horseradish peroxidase (HRP), in a water based microcapsule delivery system and demonstrates the utility of this delivery system for proteins. Aqueous solutions (1 mg/mL) of the enzyme were separately blended with aqueous solutions of the neutral sodium salt of the anionic polymer carrageenan (0.6 mM in repeat unit). These blends were instilled as uniform microdroplets into aqueous solutions of a series of eleven mono-, di-, or oligoamines (as neutral hydrochloride or acetate salts). Essentially instantaneous salt exchange interaction of the sodium salt of anionic polymer with amine hydrochloride resulted in formation of microparticles of amine/polymer complex. The enzyme was captured in the resulting capsules. The particles were washed by repeated centrifugation and resuspension in water and their particle size distribution was determined. HRP in washed pelleted microspheres was analyzed for fragmentation/aggregation by SDS-PAGE and size exclusion chromatography, for unfolding by fluorescence spectroscopy, and for specific enzymatic activity, capture efficiency and release studies by absorbance spectroscopy. Dependent on amine employed, capture efficiencies ranged from 1 to 72%. Encapsulation produced no adverse effect on protein size as no molecular fragments or aggregates were visible below or above 44 kDa. The tryptophan fluorescence spectrum of the protein did not change after encapsulation indicating no conformational change in tertiary structure. There was an apparent substrate diffusion related reduction in activity of encapsulated HRP, but almost 100% of activity was recovered on lysis of the capsules. It is concluded that water based charged film encapsulation used as a drug delivery system for proteins does not alter structural conformation or specific activity of the model protein tested and provides protein release at a constant rate.