Abstract
In this paper, the kinetic parameters of free and encapsulated enzymes in the calcium alginate-clay beads were determined using Lineweaver-Burk plot. The Michaelis constant, Kmof free alpha-amylase, glucoamylase and cellulase were 2.0831, 1.8326 and 7.8592 mg/mL, respectively, whereas for the encapsulated system, the Kmvalues were 3.1604, 2.1708 and 9.2791 mg/mL, respectively. The results showed encapsulation enzymes gave higher Kmvalue than the free enzymes. Comparatively the encapsulated alpha-amylase was 1.5 times higher and the glucoamylase and cellulase were 1.18 times higher. This suggests that the affinity of encapsulated enzymes for substrate was lower which might be due to the diffusional limitation of the substrate and enzymes. Amongst the three in both systems, glucoamylase was determined to have highest affinity followed by alpha-amylase and cellulase enzymes.
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