Literature DB >> 33505092

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.   

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 non-magnetic 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. © Association of Microbiologists of India 2020.

Entities:  

Keywords:  Bisphenol A; Enzyme immobilization; Magnetic nanoparticle; Reusability; Rhus vernicifera laccase; Stability

Year:  2020        PMID: 33505092      PMCID: PMC7810807          DOI: 10.1007/s12088-020-00912-4

Source DB:  PubMed          Journal:  Indian J Microbiol        ISSN: 0046-8991            Impact factor:   2.461


  34 in total

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