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Chlorpyrifos, one of the common broad-spectrum insecticides, can damage the human nerve system – even to the point of death under long-term exposure. In addition, chlorpyrifos is hard to be naturally degraded because of its strong combination with soil particles and long half-life. So repairing the polluted soil is urgently needed. In this study, the embedding and crosslinking immobilization techniques were used to determine the degradation of chlorpyrifos in soil. After 16SrDNA analysis, the results showed that LLBD2 is Bacillus cereus and LLBD4 is bacillus sp., and bacteria immobilized on the degradation of chlorpyrifos were significantly better than the free bacteria. The degradation rate reached 83.28% after LLBD2 being immobilized within 72 h. Furthermore, the environmental factors influenced with LLBD2 showed that immobilized bacteria were more adapted to the changed environment than the free one. Although the initial concentration, pH, and temperature were significantly changed, the degradation rate of chlorpyrifos by immobilized bacteria was stable, suggesting that environmental factors had little influence on the immobilized bacteria.
The present study used the method of embedding-adsorption to immobilize fungal laccase and to determine the suitable conditions of immobilization by measuring various activities of immobilized laccase. In addition, the immobilized laccase was further employed to repair the carbofuran-contaminated soil, and then the degradation rates of carbofuran were measured under different conditions. The experimental results showed that the appropriate conditions of embedding-adsorption were presented as follows: the weight of powdered active carbon (PAC) was 0.4 g, the concentration of CaCl₂ was 1.5%, the volume of crude laccase was 80 ml, and the immobilized time was 6 h. After 48 h, the degradation rate of carbofuran in soil could reach almost 86% by the immobilized laccase. In fact, the artificially polluted soil and polluted soils in the environment have many differences, so the coming experiment will be concentrated directly on contaminated soil based on laboratory studies in order to investigate the influence of various factors on in-situ remediation.
The mannose-binding agglutinin from bulbs of Lycoris aurea (LAA) agglutinates rabbit but not human erythrocytes. The molecular mass of the monomer in SDS/PAGE is 12 kDa while the apparent molecular mass in gel filtration is 48 kDa, indicating that LAA is a homotetramer. The full-length cDNA of LAA contains 683 bp with an open reading frame encoding a protomer of 162 amino-acid residues. Hydrophobic Cluster Analysis and molecular modeling of the 109-residue mature polypeptide suggested a similar secondary and tertiary structure to those of Narcissus pseudonarcissus agglutinin (NPA). Molecular docking revealed that, besides the three mannose-binding sites common among Amaryllidaceae lectins, LAA also contains a fourth unique mannose-binding site formed by a tryptophan cluster. The existence of four mannose-binding sites in each monomer of LAA is very unusual and has only been reported for NPA earlier.
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