Complexation and Characterization of -Amylase with Hydroxypropyl - Cyclodextrin

Drug-β cyclodextrin inclusion complexes had been an important tool for improving the solubility and bioavailability of drugs. The aim of the present research was to exploit the feasibility by using complexed enzymes (therapeutic proteins) as an alternate method for immobilization. Such complexed product was assumed to enhance the enzymatic activity. In the present study, α-Amylase (digestive enzyme) is used along with hydroxyl propyl β-cyclodextrin (HP- β-CD) to improve stability, solubility and bioavailability of enzyme. In the present study, different molar ratios of α-Amylase and cyclodextrin were prepared with different contact period between guest and host molecule to allow complexation, and interference of HP- β-CD on enzymatic activity of α-amylase was also studied. The prima facei evidence indicates that enzyme activity was decreased, when α-amylase was complexed with increasing concentrations of HP-β-CD. Solid inclusion complex was prepared by precipitation method at isoelectric point (pH 4.6). The complex was characterized by UV spectrophotometric and FT-IR technique. The presence of α-amylase and HP-β-CD in the complex was observed, it indicates that the enzyme activity was decreased in presence of HP-β-CD. High temperature studies, acid media studies (mimicking GIT) and accelerated studies need to be explored for concluding the role of inclusion complexes in the therapy.