Fabrication of Fe3O4@SiO2@PDA-Ni2+ nanoparticles for one-step affinity immobilization and purification of His-tagged glucose dehydrogenase

Huang, Jiaying; Shen, Yu; Li, Ruifang; Han, Keke; Zhang, Ye-Wang

doi:10.1016/j.procbio.2023.02.024

Cited by 4 publications

(1 citation statement)

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“…Specifically, we focused on the use of magnetic Ni 0.4 Cu 0.5 Zn 0.1 Fe 2 O 4 nanoparticles, which were prepared using an advanced, convenient, simple, and rapid combustion process. To enhance the nanoparticles' functionality, a SiO 2 functional layer was applied to their surface using sodium silicate [63,64]. The modification process with sodium silicate introduced a substantial amount of Si-OH groups on the surface of the nanoparticles.…”

Section: Introductionmentioning

confidence: 99%

Enhanced catalytic performance of penicillin G acylase by covalent immobilization onto functionally-modified magnetic Ni0.4Cu0.5Zn0.1Fe2O4 nanoparticles

Lv,

Wang,

et al. 2024

PLoS ONE

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With the emergence of penicillin resistance, the development of novel antibiotics has become an urgent necessity. Semi-synthetic penicillin has emerged as a promising alternative to traditional penicillin. The demand for the crucial intermediate, 6-aminopicillanic acid (6-APA), is on the rise. Enzyme catalysis is the primary method employed for its production. However, due to certain limitations, the strategy of enzyme immobilization has also gained prominence. The magnetic Ni0.4Cu0.5Zn0.1Fe2O4 nanoparticles were successfully prepared by a rapid-combustion method. Sodium silicate was used to modify the surface of the Ni0.4Cu0.5Zn0.1Fe2O4 nanoparticles to obtain silica-coated nanoparticles (Ni0.4Cu0.5Zn0.1Fe2O4-SiO2). Subsequently, in order to better crosslink PGA, the nanoparticles were modified again with glutaraldehyde to obtain glutaraldehyde crosslinked Ni0.4Cu0.5Zn0.1Fe2O4-SiO2-GA nanoparticles which could immobilize the PGA. The structure of the PGA protein was analyzed by the PyMol program and the immobilization strategy was determined. The conditions of PGA immobilization were investigated, including immobilization time and PGA concentration. Finally, the enzymological properties of the immobilized and free PGA were compared. The optimum catalytic pH of immobilized and free PGA was 8.0, and the optimum catalytic temperature of immobilized PGA was 50°C, 5°C higher than that of free PGA. Immobilized PGA in a certain pH and temperature range showed better catalytic stability. Vmax and Km of immobilized PGA were 0.3727 μmol·min-1 and 0.0436 mol·L-1, and the corresponding free PGA were 0.7325 μmol·min-1 and 0.0227 mol·L-1. After five cycles, the immobilized enzyme activity was still higher than 25%.

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Section: Introductionmentioning

confidence: 99%

Enhanced catalytic performance of penicillin G acylase by covalent immobilization onto functionally-modified magnetic Ni0.4Cu0.5Zn0.1Fe2O4 nanoparticles

Lv,

Wang,

et al. 2024

PLoS ONE

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Production of recombinant β-glucosidase and simultaneous immobilization and purification using immobilized metal ion affinity membrane

Gu,

Nargotra,

Kuo

et al. 2024

Journal of the Taiwan Institute of Chemical Engineers

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Removal and measurement of trace amounts of rhodamine B in aqueous samples based on the synthesis of a nanosorbent composed of Fe₃O₄ nanoparticles modified with SiO₂ and polydopamine by magnetic solid phase extraction

Yari,

Salemzadeh

2024

Anal. Methods

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Fabrication of Fe3O4@SiO2@PDA-Ni2+ nanoparticles for one-step affinity immobilization and purification of His-tagged glucose dehydrogenase

Cited by 4 publications

References 52 publications

Enhanced catalytic performance of penicillin G acylase by covalent immobilization onto functionally-modified magnetic Ni0.4Cu0.5Zn0.1Fe2O4 nanoparticles

Enhanced catalytic performance of penicillin G acylase by covalent immobilization onto functionally-modified magnetic Ni0.4Cu0.5Zn0.1Fe2O4 nanoparticles

Production of recombinant β-glucosidase and simultaneous immobilization and purification using immobilized metal ion affinity membrane

Removal and measurement of trace amounts of rhodamine B in aqueous samples based on the synthesis of a nanosorbent composed of Fe₃O₄ nanoparticles modified with SiO₂ and polydopamine by magnetic solid phase extraction

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Fabrication of Fe3O4@SiO2@PDA-Ni2+ nanoparticles for one-step affinity immobilization and purification of His-tagged glucose dehydrogenase

Cited by 4 publications

References 52 publications

Enhanced catalytic performance of penicillin G acylase by covalent immobilization onto functionally-modified magnetic Ni0.4Cu0.5Zn0.1Fe2O4 nanoparticles

Enhanced catalytic performance of penicillin G acylase by covalent immobilization onto functionally-modified magnetic Ni0.4Cu0.5Zn0.1Fe2O4 nanoparticles

Production of recombinant β-glucosidase and simultaneous immobilization and purification using immobilized metal ion affinity membrane

Removal and measurement of trace amounts of rhodamine B in aqueous samples based on the synthesis of a nanosorbent composed of Fe3O4 nanoparticles modified with SiO2 and polydopamine by magnetic solid phase extraction

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Removal and measurement of trace amounts of rhodamine B in aqueous samples based on the synthesis of a nanosorbent composed of Fe₃O₄ nanoparticles modified with SiO₂ and polydopamine by magnetic solid phase extraction