Rhus vernicifera Laccase Immobilization on Magnetic Nanoparticles to Improve Stability and Its Potential Application in
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ORIGINAL RESEARCH ARTICLE
Rhus vernicifera Laccase Immobilization on Magnetic Nanoparticles to Improve Stability and Its Potential Application in Bisphenol A Degradation Sanjay K. S. Patel1 • Rahul K. Gupta1 • Sang-Yong Kim2 • In-Won Kim1 Vipin C. Kalia1 • Jung-Kul Lee1
•
Received: 28 July 2020 / Accepted: 13 October 2020 Ó Association of Microbiologists of India 2020
Abstract In the present study, Rhus vernicifera laccase (RvLac) was immobilized through covalent methods on the magnetic nanoparticles. Fe2O3 and Fe3O4 nanoparticles activated by 3-aminopropyltriethoxysilane followed with glutaraldehyde showed maximum immobilization yields and relative activity up to 81.4 and 84.3% at optimum incubation and pH of 18 h and 5.8, respectively. The maximum RvLac loading of 156 mg/g of support was recorded on Fe2O3 nanoparticles. A higher optimum pH and temperature of 4.0 and 45 °C were noted for immobilized enzyme compared to values of 3.5 and 40 °C for free form, respectively. Immobilized RvLac exhibited better relative activity profiles at various pH and temperature ranges. The immobilized enzyme showed up to 16-fold improvement in the thermal stability, when incubated at 60 °C, and retained up to 82.9% of residual activity after ten cycles of reuses. Immobilized RvLac exhibited up to 1.9-fold higher bisphenol A degradation efficiency potential over free enzyme. Previous reports have demonstrated the immobilization of RvLac on nonmagnetic supports. This study has demonstrated that immobilization of RvLac on magnetic nanoparticles is very efficient especially for achieving high loading, better pH and temperature profiles, and thermal- and solvents-stability, high reusability, and higher degradation of bisphenol A.
& Jung-Kul Lee [email protected] 1
Department of Chemical Engineering, Konkuk University, 1 Hwayang-Dong, Gwangjin-Gu, Seoul 05029, Republic of Korea
2
Department of Food Science and Biotechnology, Shin-Ansan University, Ansan 15435, Republic of Korea
Keywords Bisphenol A Enzyme immobilization Magnetic nanoparticle Reusability Rhus vernicifera laccase Stability
Introduction Biocatalysts have been widely used for biotransformation applications such as industrial and environmental sectors [1, 2]. The enzymes as cell-free biocatalysts are founded more desirable to use in bioconversion reactions due to their high specificity towards substrate and reaction rate, easy in product separation, and tolerance towards higher substrate concentration, and solvents [3–5]. Primarily, the uses of the enzyme are limited due to their high cost and low stability. Various strategies have been employed to improve enzyme properties through the selection of suitable microbial sources, protein engineering, and immobilization [6–9]. The immobilization of biocatalysts in the form of either whole-cells or enzymes has been widely demonstrated to enhance their stability during biotransformation [10–14]. The enzyme’s properties such as activity and stability are significantly varied after immobilization on supports [11,
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