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Investigation of deactivation thermodynamics of lipase immobilized on polymeric carrier
- Badgujar, Kirtikumar C., Bhanage, Bhalchandra M.
- Bioprocess and biosystems engineering 2017 v.40 no.5 pp. 741-757
- Candida rugosa, Gibbs free energy, biocatalysts, carboxylic ester hydrolases, catalytic activity, chitosan, crosslinking, economic sustainability, enthalpy, entropy, half life, polyvinyl alcohol, solvents, temperature
- In the present work, we have investigated biochemical thermo-kinetic stability of lipases immobilized on a biocompatible polymeric material. Immobilization of lipase Candida rugosa (CRL) was carried out on biocompatible blend of poly vinyl alcohol (PVA) and chitosan (CHY) support via entrapment and glutardehyde (Glu) cross-linking method to produce PVA:CHY:CRL and PVA:CHY:Glu:CRL as robust biocatalyst. These immobilized lipases were characterized by various physico-biochemical characterization techniques. Later on, thermal and solvent stability of polymer immobilized lipase was determined in term of half-life time (t ₀.₅), D values, enthalpy (ΔH°), entropy (ΔS°), and free energy (ΔG°) of deactivation at different temperatures and in various solvents. The thermodynamic deactivation stability trend was found as: cross-linked lipase CRL > entrapped lipase CRL > free lipase CRL. Moreover, kinetic parameters, such as K ₘ, V ₘₐₓ, and catalytic efficiency, were also determined to understand the kinetic features. The polymer immobilized enzyme was reused to investigate the economic viability of the developed biocatalyst.