Low enzyme activity is one of the disadvantages of immobilized laccase. In this study, waste Cu-loaded activated carbon (Cu-AC) was successfully used in preparing a novel composite support,cellulose / Cu-loaded activated carbon beads (C / Cu-AC), and effectively boosted immobilized laccase activity. To achieve optimum conditions for immobilization of laccase, the immobilization time, pH and laccase concentration were examined. The highest immobilized laccase activity (34.21 U/g) was achieved under optimum conditions (T = 4 h, pH = 4, C = 5 g/L), which was increased by 35.86 % compared to control. In addition, the immobilized laccase showed an outstanding performance in thermostability and reusability compared to free laccase. Moreover, the degradation of BPA by immobilized laccase was carried out, and the optimum degradation conditions were explored. Under such conditions: concentration of BPA was 75 mg / L and pH = 4, t = 1 h, T = 50 °C,the removal yield of BPA reached a maximum of 79.88 %. Therefore, the utilization of waste Cu-CA is a powerful method to boost immobilized laccase activity and creating a new way to high value treatment of waste Cu-CA.
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http://dx.doi.org/10.1016/j.ijbiomac.2024.136121 | DOI Listing |
Sci Rep
January 2025
Faculty of Biotechnology, German International University, Regional Ring Road, East Cairo, New Administrative Capital, Cairo, Egypt.
In the current study, calcium alginate was used as a carrier for Agaricus bisporus CU13 laccase immobilization, with an immobilization yield of the entrapped laccase of 91.95%. Free and immobilized enzymes showed their best enzyme activity at 60 °C as an optimum temperature.
View Article and Find Full Text PDFInt J Biol Macromol
December 2024
Pharmaceutical Sciences Research Center, Hemoglobinopathy Institute, Mazandaran University of Medical Sciences, P.O. Box 48175-861, Sari 4847193698, Iran; Thalassemia Research Center, Hemoglobinopathy Institute, Mazandaran University of Medical Sciences, Sari, Iran. Electronic address:
The environmental persistence of pharmaceuticals represents a significant threat to aquatic ecosystems and human health, while limitations in conventional wastewater treatment methods underscore the urgent need for innovative and eco-friendly degradation strategies. Photobiocatalytic approaches provide a promising solution for the effective degradation of pharmaceutical contaminants by harnessing the synergistic effects of both photocatalysts and biocatalysts. In this study, we developed a photobiocatalytic composite by co-immobilizing laccase enzyme and zinc oxide nanoparticles on bacterial cellulose synthesized from orange peel waste.
View Article and Find Full Text PDFJ Xenobiot
December 2024
Department of Chemical Engineering, University of Pretoria, Pretoria 0028, South Africa.
The direct discharge of cationic surfactants into environmental matrices has exponentially increased due to their wide application in many products. These compounds and their degraded products disrupt microbial dynamics, hinder plant survival, and affect human health. Therefore, there is an urgent need to develop electroanalytical assessment techniques for their identification, determination, and monitoring.
View Article and Find Full Text PDFACS Appl Mater Interfaces
December 2024
Key Laboratory of Engineering Biology for Low-carbon Manufacturing, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin 300308, P. R. China.
Enzymatic fuel cells (EFCs) are emerging as promising technologies in renewable energy and biomedical applications, utilizing enzyme catalysts to convert the chemical energy of renewable biomass into electrical energy, known for their high energy conversion efficiency and excellent biocompatibility. Currently, EFCs face challenges of poor stability and catalytic efficiency at the cathodes, necessitating solutions to enhance the oriented immobilization of multicopper oxidases for improved heterogeneous electron transfer efficiency. This study successfully identified a surface-binding peptide (SBP, 13 amino acids) derived from a methionine-rich fragment (MetRich, 53 amino acids) in CueO through semirational design.
View Article and Find Full Text PDFIndian J Microbiol
December 2024
Department of Bio and Nano Technology, Guru Jambheshwar University of Science and Technology Hisar, Haryana, 124001 India.
Laccase is an extracellular enzyme that is widely used in the decolonization of textile dyes in waste water. The aim of our study was to isolate, purify, characterize and immobilize the laccase enzyme produced by HBB 7328. Purified laccase enzyme was immobilized in polyacrylamide gel to explore its ability in decolonization of textile dyes.
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