Catalytic, Kinetic, and Thermodynamic Properties of Pleurotus Ostreatus NRRL 3501 Laccase Immobilized on Clinoptilolite Nanoparticles and its Application in Dye Decolorization | ||
| Egyptian Journal of Chemistry | ||
| Volume 67, Issue 13, December 2024, Pages 461-469 PDF (540.72 K) | ||
| Document Type: Original Article | ||
| DOI: 10.21608/ejchem.2024.257870.9052 | ||
| Authors | ||
| Hala R. Wehaidy* 1; Shireen A. Saleh1; Walaa A. Abdel Wahab1; Samia A. Ahmed1; Hanan F. Youssef2; Heba M. El-Hennawi3; Mohamed A. Abdel-Naby1 | ||
| 1Chemistry of Natural and Microbial products Department, National Research Centre, Dokki, Giza, Egypt. | ||
| 2Refractories, Ceramics and Building Materials Department, National Research Centre, Dokki, Giza, Egypt. | ||
| 3Dyeing, Printing and Textile Auxiliaries Department, National Research Centre, Dokki, Giza, Egypt. | ||
| Abstract | ||
| Laccase from Pleurotus ostreatus was immobilized on different nanoparticles by physical adsorption and covalent binding. The immobilized enzyme on Na-clinoptilolite nanoparticles showed the highest recovered activity (71.75%) and thermal stability. X-Ray diffraction, surface morphology and the internal structure of the immobilization carrier (Na-clinoptilolite nanoparticles) were investigated. Compared to the free enzyme, the immobilized preparation exhibited higher optimum temperature, lower activation energy (Ea), lower deactivation constant rate (kd), higher t1/2 and higher decimal reduction time values (D) within the temperature range of 50–70◦C. The thermodynamic parameters (ΔH*, ΔG*, ΔS*) of irreversible thermal denaturation for the free and immobilized laccase were also evaluated. The values of enthalpy of activation (ΔH*), and free energy of transition state binding (ΔG*E−T) for substrate catalysis were lowered for the immobilized enzyme. Moreover, there was highly significant impact on improving the values of Vmax/Km, kcat, kcat/Km, and ΔG*E−S for the immobilized enzyme. The immobilized laccase from Pleurotus ostreatus NRRL 3501 on Na-clinoptilolite nanoparticles was evaluated for dye decolorization. In batch experiments the immobilized enzyme was able to decolorize the following dyes R. Blue 203 (97%), A. red 299 (100%), and Acid mix (89%) after incubation for 120 min. In repeated use the immobilized enzyme was able to decolorize the dye for 8 continuous cycles. | ||
| Keywords | ||
| Laccase immobilization; Zeolite nanoparticles; sodium-clinoptilolite pellets; dye decolorization | ||
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