Chicken Feather Derived Novel Support Material for Immobilization of Laccase and Its Application in Oxidation of Veratryl Alcohol

Abstract

Application of a biocatalyst at an industrial scale primarily depends on its intrinsic properties, the nature of the support materials, and the scalability of the catalyst. Support materials play an important role in the biocatalytic performance with their mechanical and thermal properties, accessibility, nontoxicity, and ease of derivatization for immobilizion of enzyme. Chicken feather, a readily available poultry waste material, was processed and modified for enzyme immobilization. Free Trametes maxima laccase (TML) was immobilized on the amino-functionalized chicken feather particles (TML@ACFP), and an immobilization yield of 74.24% was achieved. Immobilization improved the pH optimum from 3.0 (TML) to 4.1 (TML@ACFP) and temperature optimum by 5 °C. The kinetics and thermodynamics of thermal inactivation of free TML and immobilized TML@ACFP were studied over the temperature range from 55 to 65 °C. The apparent half-life (t 1/2 ) and decimal reduction time (D-value) for TML was found to be 154.9 and 514.8 min and 256.8 and 853.3 min for TML@ACFP, respectively, at 55 °C. The activation energy for deactivation (E d ) was found to be 117.48 and 137.85 kJ/mol for TML and TML@ACFP, respectively. Gibbs free energy (?G) and change in enthalpy (?H) were increased from 106.58 and 114.75 kJ/mol for TML to 107.96 and 135.12 kJ/mol for TML@ACFP, respectively, demonstrating its higher stability. The biocatalytic transformation was performed with TML@ACFP for the oxidation of lignin model compound veratryl alcohol. So far, this is the first strategy that uses chicken feather waste derived novel support material for immobilization of enzyme and its application in the biotransformation. © 2018 American Chemical Society.