School Of Environment And Earth Sciences
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Item Amino-functionalized Magnetic Iron Nanoparticles As a Carrier for Laccase Enzyme and Its Potential to Degrade Chlorpyrifos in Contaminated Soil: Fate and Kinetics(Springer Science and Business Media Deutschland GmbH, 2022-04-14T00:00:00) Das, Anamika; Yogalakshmi, KnThe present study utilizes the covalent-crosslinking method to immobilize the�laccase enzyme on magnetic iron nanoparticles�and further assess its potential in degrading�chlorpyrifos in pesticide spiked�soil. The soil texture analysis revealed the presence of clay, silt and sand accounting to�7.1%, 14.3%, and 78.6%, respectively. The degradation of chlorpyrifos in spiked soil�using laccase enzyme�immobilized�magnetic iron nanoparticles was measured for 60�days�in a batch process. The results revealed a gradual increase in degradation efficiency showing around�29.3%, 43.8%, 56.3%, and 67.3% at the 20th, 30th, 40th, and 50th day�of incubation. A maximum degradation of�83.6% was observed on the 60th day of incubation. Intermediate products 2,4-bis(1,1 dimethylethyl) phenol, 1,2 benzenedicarboxylic acid, bis(2-methyl propyl) ester�and�piperidine confirmed the degradation of chlorpyrifos in soil. The piperidine originated in the chromatogram between�20�40�days of incubation and diminished later. Chlorpyrifos degradation followed pseudo first-order kinetics with a R2 of 0.96. Further, the nanoparticles showed no negative�impact on soil bacterial population during the antibacterial assay. The study confirms the degradation of chlorpyrifos in contaminated soil using laccase-immobilized nanoparticles. � 2022, The Author(s), under exclusive licence to Springer Nature Switzerland AG.Item Comparative Analysis of Laccase Immobilization on Magnetic Iron Nanoparticles using Two Activating Agents:EDAC and Cyanuric Chloride(Tamil Nadu Scientific Research Organization (TNSRO), 2016) Das, Anamika; Singh, Jatinder; Yogalakshmi, K. N.Surface modification improves the covalent bonding of enzymes onto the magnetic nanoparticles. The present study aims to evaluate the effect of surface activators (EDAC (1-Ethyl-3-(3-dimethylaminopropyl) carbodiimide) and Cyanuric chloride) in immobilization of enzymes. Nanoparticles prepared by co-precipitation method ranged insize from 15-20 nm. The nanoparticles possessed crystalline property as confirmed by the XRD (X-ray powder diffraction) peaks. SEM-EDS (Scanning Electron Microscopy- Energy Dispersive X-ray Spectroscopy) analysis of EDAC and cyanuric acid activated nanoparticles showed atomic sulphur percent of 0.08% and 0.02%, respectively. It is concluded that EDACwas more successful in loading more enzymes than cyanuric acid. Bradford estimation of the unbound protein after first wash for ENP-EDAC and ENP-CC was 29.1 μg/mL and 132.1 μg/mL, respectively. EDAC is a potential surface modifier for enzyme immobilization process.