Biocatalytic degradation technology has received a great deal of attention in water treatment because of its advantages of high efficiency, environmental friendliness, and no secondary pollution. Herein, for the first time, horseradish peroxidase and mediator syringaldehyde were co-immobilized into functionalized calcium alginate composite beads grafted with glycidyl methacrylate and dopamine. The resultant biocatalyst of the co-immobilized horseradish peroxidase-syringaldehyde system has displayed excellent catalytic performance to degrade indole in water. The degradation rate of 100% was achieved in the presence of hydrogen peroxide even if the indole concentration was changing from 25 mg/L to 500 mg/L. If only the free enzyme was used under the identical water treatment conditions, the degradation of indole could hardly be observed even when the concentration of indole is low at 25 mg/L. This was attributed to the effective co-immobilization of the enzyme and the mediator so that the catalytic activity of horseradish peroxidase and the synergistic catalytic action of syringaldehyde could be fully developed. Furthermore, while the spherical catalyst was operated in succession and reused for four cycles in 50 mg/L indole solution, the degradation rate remained 91.8% due to its considerable reusability. This research demonstrated and provided a novel biocatalytic approach to degrade indole in water by the co-immobilized horseradish peroxidase-syringaldehyde system as biocatalyst.
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http://dx.doi.org/10.1016/j.chemosphere.2020.128411 | DOI Listing |
Int J Biol Macromol
January 2025
School of Light Industry and Chemical Engineering, Dalian Polytechnic University, Dalian 116034, China. Electronic address:
Accurate, specific, and cost-effective detection of toxic cyanogenic glycosides is crucial for ensuring biological health and food safety. In this study, a novel biosensor based on co-immobilized multi-enzyme system was constructed by artificial antibody-antigen-directed immobilization for the colorimetric detection of amygdalin through a cascade reaction catalyzed by β-glucosidase, glucose oxidase, and horseradish peroxidase. Artificial antibodies and antigens were prepared using catechol and 3,4-dihydroxybenzaldehyde, respectively, to generate mutual affinity recognition ability for enzyme immobilization.
View Article and Find Full Text PDFInt J Biol Macromol
December 2024
College of Pharmaceutical Science, Hebei University, Baoding 071002, China; Key Laboratory of Pharmaceutical Quality Control of Hebei Province, College of Pharmaceutical Science, Hebei University, Baoding 071002, China; State Key Laboratory of New Pharmaceutical Preparations and Excipients, Key Laboratory of Medicinal Chemistry and Molecular Diagnosis of Ministry of Education, Hebei University, Baoding 071002, China. Electronic address:
In traditional multienzyme random co-immobilization, it is difficult to precisely locate and regulate the relative positions between two enzyme molecules, resulting in low cascade efficiency between the two enzymes and limiting the application of multienzyme cascade catalysis technology. This study prepared PVAC@Y-dsDNA@GOD/HRP magnetic co-immobilized multienzyme by constructing a three-pronged DNA scaffold for co-coupling glucose oxidase (GOD) and horseradish peroxidase (HRP), which achieved directional co-immobilization of dual enzymes and precise regulation of inter-enzyme distance. Compared with traditional random co-immobilization of multienzyme, PVAC@Y-dsDNA@GOD/HRP could shorten the distance between GOD and HRP to the nanoscale and form substrate channeling, which greatly improved the cascade activity between the two enzymes.
View Article and Find Full Text PDFInt J Biol Macromol
July 2024
Key Laboratory of Analytical Chemistry for Life Science of Shaanxi Province, School of Chemistry and Chemical Engineering, Shaanxi Normal University, 620 West Chang'an Street, Xi'an 710119, China. Electronic address:
Surface chemistry of carriers plays a key role in enzyme loading capacity, structure rigidity, and thus catalyze activity of immobilized enzymes. In this work, the two model enzymes of horseradish peroxidase (HRP) and glucose oxidase (GOx) are co-immobilized on the lysozyme functionalized magnetic core-shell nanocomposites (LYZ@MCSNCs) to enhance their stability and activity. Briefly, the HRP and GOx aggregates are firstly formed under the crosslinker of trimesic acid, in which the loading amount and the rigidity of the enzyme can be further increased.
View Article and Find Full Text PDFJ Colloid Interface Sci
October 2024
Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, School of Life Sciences, Jilin University, Changchun 130012, China; Center for Supramolecular Chemical Biology, Jilin University, Changchun 130012, China. Electronic address:
Formate is an important environmental pollutant, and meanwhile its concentration change is associated with a variety of diseases. Thus, rapid and sensitive detection of formate is critical for the biochemical analysis of complex samples and clinical diagnosis of multiple diseases. Herein, a colorimetric biosensor was constructed based on the cascade catalysis of formate oxidase (FOx) and horseradish peroxidase (HRP).
View Article and Find Full Text PDFChemosphere
June 2024
Department of Civil Infrastructure and Environmental Engineering, Khalifa University, PO Box, 127788, Abu Dhabi, United Arab Emirates. Electronic address:
This research reported on the immobilization of environmentally friendly enzymes, such as horseradish peroxidase (HRP) and laccase (L), along with the hydrophilic zwitterionic compound l-DOPA on nano-filtration (NF) membranes. This approach introduced biocatalytic membranes, leveraging combined effects between membranes and enzymes. The aim was to systematically assess the efficacy of the enzymatic modified membrane (HRP-NF) in degrading colors in the wastewater, as well as enhancing the membrane resistance toward organic fouling.
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