Nanoclay Supporting Materials for Enzymes Immobilization: Kinetics Investigation of Free and Immobilized System

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, K_m of free alpha-amylase, glucoamylase and cellulase were 2.0831, 1.8326 and 7.8592 mg/mL, respectively, whereas for the encapsulated system, the K_m values were 3.1604, 2.1708 and 9.2791 mg/mL, respectively. The results showed encapsulation enzymes gave higher K_m value 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.

• Periodical: Applied Mechanics and Materials (Volume 393)
• Pages: 115-120
• DOI: https://doi.org/10.4028/www.scientific.net/AMM.393.115
• Online since: September 2013
• Authors: Siti Noraida Abd Rahim, Alawi Sulaiman, Ku Halim Ku Hamid, Miradatul Najwa Mohd Rodhi, Musa Mohibah, Fazlena Hamzah, Nurul Aini Edama
• Keywords: Calcium Alginate-Clay, Encapsulation, Enzymes, Kinetic Parameter, Tapioca Slurry

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