4.7 Article

Optimization strategy for laccase immobilization on polyethylene terephthalate grafted with maleic anhydride electrospun nanofiber mat

Journal

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 166, Issue -, Pages 876-883

Publisher

ELSEVIER
DOI: 10.1016/j.ijbiomac.2020.10.244

Keywords

Lactase; Immobilization; Nanofiber; Optimization

Funding

  1. Universiti Teknologi Malaysia (UTM)
  2. Fundamental Research Grant Scheme [FRGS] [R.J130000.7851.5F210]

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The study optimized the immobilization of laccase on PET-g-MAH ENM, showing a significant increase in immobilization yield under specific conditions, with the immobilized laccase demonstrating good activity across a wide range of pH and temperature conditions.
Enzyme immobilization has been known to be one of the methods to improve the stability and reusability of enzyme. In this study, a strategy to optimize laccase immobilization on polyethylene terephthalate grafted with maleic anhydride electrospun nanofiber mat (PET-g-MAH ENM) was developed. The development involves the screening and optimization processes of the crucial factors that influence the immobilization yield such as enzyme concentration, pH values, covalent bonding (CV) time, CV temperature, crosslinking (CL) time. CL temperature and glutaraldehyde concentration using two-level factorial design and Box-Behnken design (BOW, respectively. It was found that laccase concentration, pH values and glutaraldehyde concentration play important role in enhancing the immobilization yield of laccase on PET-g-MAH ENM in the screening process. Subsequently, the optimization result showed at 028 mg/mIlaccase concentration, pH 3 and 0.45% (v/v) glutaraldehyde concentrations gave the highest immobilization yield at 87.64% which was 812% increment from the immobilization yield before optimization. Under the optimum condition, the immobilized laccase was able to oxidize 2, 2-azinobis 3-ethylbenzothiazol ine-6- sulfonic acid (ARTS) in a broad range of pH (pH 3-6) and temperature (20- 70 degrees C). Meanwhile, the kinetic parameters for K-m and V-max) , were 1.331 mM and 0.041 mM/min, respectively. It was concluded that the optimization of immobilized laccase on PET-g-MAH ENM enhance the performance of this biocatalyst. (C) 2020 Elsevier B.V. All rights reserved.

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