Abstract
Papain, a proteolytic enzyme was purified from latex of Carica papaya by a variety of techniques such as two-step salt precipitation, organic solvent precipitation (ethanol) and ion exchange chromatography. Fold purity obtained using ion exchange chromatography was in the range of 4.5 to 5 times as compared to the precipitation techniques. The purified papain was entrapped in ionotropically cross-linked alginate beads, in order to develop formulation for site-specific delivery of papain in intestine. The entrapment efficiency for papain in alginate beads was found to be in excess of 86%. Drying at low temperature and low air velocity results into maximum retention of papain activity; however, drying time increases significantly. The dissolution study shows the possible use of alginate beads for site-specific intestinal delivery of papain. The shelf-life of papain can be improved significantly by entrapment in alginate matrix, which was confirmed by an FTIR study.
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