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 (ΔG) and change in enthalpy (ΔH) 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.

Evaluation of MxOy/fucoidan hybrid system and their application in lipase immobilization process

“…In recent decades, development of inexpensive, biodegradable, and easily available natural materials in different application have been of more interest for the huge number of researchers. It is highly preferable that the carrier matrix that binds the enzyme can be produced reproducibly and does not disrupt the enzyme activity, because it has a great importance for technological performance and commercial success 1 – 3 . However, those materials also have some disadvantages (low mechanical strength and limited thermal stability) which can be improved using appropriate modification process 4 , 5 .…”

Rhus vernicifera Laccase Immobilization on Magnetic Nanoparticles to Improve Stability and Its Potential Application in Bisphenol A Degradation

“…RvLac showed half-life (t 1/2 ) of * 13 min at 60 8C as compared to t 1/2 values of 12 min for T. versicolor [17], and * 20 min for bacterial laccase from c-Proteobacterium JB [49]. The immobilized laccase on the chicken feather showed t 1/2 activity of 134 min over free enzyme (109 min) at 60 °C [30]. In contrast, free and immobilized bacterial laccase from c-Proteobacterium JB on nitrocellulose membrane showed similar temperature stability at 60 8C [49].…”

“…Commercially available enzymes such as glucose oxidase [21], horseradish peroxidase [17], lipase [23], and laccase [29,30] have been widely demonstrated for their immobilization on nanomaterials. Laccase is a multi-copper oxidase that catalyzes the oxidation of phenolics, and non-phenolics compounds [10,31,32].…”

Fungal Laccases: The Forefront of Enzymes for Sustainability

“…Chicken feathers are a waste by-product of the poultry industry. Common disposal methods are harmful for the environment and include incineration or burial in landfills [133]. Suman et al [134] covalently immobilized a LC from T. maxima with chicken feathers that were functionalized with amino 3-aminopropyltrimethoxysilane.…”