Abstract
A Nocardiopsis sp. stain B2 with an ability to produce stable α-amylase was isolated from marine sediments. The characterization of microorganism was done by biochemical tests and 16S rDNA sequencing. The α-amylase was purified by gel filtration chromatography by using sephadex G-75. The molecular mass of the amylase was found to be 45kDa by SDS-PAGE and gel filtration chromatography. The isolated α-amylase was immobilized by ionotropic gelation technique using gellan gum (GG). These microspheres were spherical with average particle size of 375.62±21.76 to 492.54±32.18μm. The entrapment efficiency of these α-amylase loaded GG microspheres was found 74.76±1.32 to 87.64±1.52%. Characterization of α-amylase–gellan gum microspheres was confirmed using FTIR and SEM analysis. The in vitro amylase release kinetic have been studied by various mathematical models that follow the Korsmeyer–Peppas model (R2=0.9804–0.9831) with anomalous (non-Fickian) diffusion release mechanism.
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