The production of microbial lipid using lignocellulosic agroforestry residues has attracted much attention. But, various inhibitors such as phenols and furans, which are produced during lignocellulosic hydrolysate preparation, are harmful to microbial lipid accumulation. Herein, we developed a novel detoxification strategy of rice straw hydrolysate using immobilized laccase on magnetic FeO nanoparticles for improving lipid production of Rhodotorula glutinis. Compared with free laccase, the immobilized laccase on magnetic nanoparticles showed better stability, which still retained 76% of original activity at 70 °C and 56% at pH 2 for 6 h. This immobilized laccase was reused to remove inhibitors in acid-pretreated rice straw hydrolysate through recycling with external magnetic field. The results showed that most of phenols, parts of furans, and formic acids could be removed by immobilized laccase after the first batch. Notably, the immobilized laccase exhibited good reusability in repeated batch detoxification. 78.2% phenols, 43.8% furfural, 30.4% HMF, and 16.5% formic acid in the hydrolysate were removed after the fourth batch. Furthermore, these detoxified rice straw hydrolysates, as substrates, were applied to the lipid production of Rhodotorula glutinis. The lipid yield in detoxified hydrolysate was significantly higher than that in undetoxified hydrolysate. These findings suggest that the immobilized laccase on magnetic nanoparticles has a potential to detoxify lignocellusic hydrolysate for improving microbial lipid production.
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http://dx.doi.org/10.1007/s12010-020-03465-w | 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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