无铁磁性纳米颗粒作为靶向酶固定化的新支持:钴和镍基系统

IF 2.3 4区 化学 Q3 CHEMISTRY, PHYSICAL
Graziela Paludo, Fernanda Leonhardt, Adriano Gennari, Edilson Valmir Benvenutti, Sabrina Nicolodi, Tânia Maria Haas Costa, Nathalia Denise de Moura Sperotto, Cristiano Valim Bizarro, Luiz Augusto Basso, Pablo Machado, Gaby Renard, Jocelei Maria Chies, Giandra Volpato, Claucia Fernanda Volken de Souza
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引用次数: 0

摘要

通过快速低成本的工艺合成的非铁磁性纳米颗粒为his标记酶的定向固定化提供了一个有前途的平台,可以从反应介质中实现高效的磁回收。在这项研究中,我们探索了一种开发无铁磁性支架的新策略的潜力,旨在提高工业过程中酶的再利用。在这里,我们报道了通过一锅法合成钴基和镍基磁性纳米颗粒,并评估了它们对Kluyveromyces sp. (HisGal)中重组his标记的β-半乳糖苷酶的靶向固定化的支持。两种载体都实现了高固定效率,最佳负载为30个Uenzyme/gsupport。结构和成分分析,包括x射线衍射、热重分析、能量色散光谱和透射红外光谱,揭示了钴纳米颗粒的优越性能,使HisGal的定向固定更加有效。在钴基或镍基纳米颗粒上固定化使β-半乳糖苷酶的最佳温度分别为40°C和50°C,并拓宽了酶活性的pH范围。固定化生物催化剂表现出更高的操作稳定性,在25次重复使用循环中保持活性,并提高了HisGal对钠、钾、镁和钙离子存在引起的热降解和抑制作用的抵抗力。此外,钴基支持显著降低半乳糖抑制和增强乳糖亲和力在脱脂牛奶系统。这些发现突出了无铁钴基和镍基磁性纳米颗粒作为酶固定化的有效载体的多功能性和生物技术潜力,提供了固定化β-半乳糖苷酶的快速有效回收,并有助于这些过程的经济可行性。图形抽象
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Iron-free magnetic nanoparticles as a novel support for targeted enzyme immobilization: cobalt- and nickel-based systems

Non-iron magnetic nanoparticles synthesized through a rapid and low-cost process present a promising platform for the oriented immobilization of His-tagged enzymes, enabling efficient magnetic recovery from the reaction medium. In this study, we explored the potential of a novel strategy for developing iron-free magnetic supports aimed at enhancing enzyme reuse in industrial processes. Here, we report the synthesis of cobalt- and nickel-based magnetic nanoparticles via one-pot methods and their evaluation as supports for the targeted immobilization of a recombinant His-tagged β-galactosidase from Kluyveromyces sp. (HisGal). Both supports achieved high immobilization efficiency, with optimal loading at 30 Uenzyme/gsupport. Structural and compositional analyses, including X-ray diffraction, thermogravimetric analysis, energy-dispersive spectroscopy, and transmission infrared spectroscopy, revealed superior performance of cobalt nanoparticles, enabling more effective oriented immobilization of HisGal. Immobilization on cobalt- or nickel-based nanoparticles shifted the optimal temperature of β-galactosidase to 40 °C and 50 °C, respectively, and broadened the pH range of enzymatic activity. The immobilized biocatalysts demonstrated enhanced operational stability, maintaining activity over 25 reuse cycles, and improved the resistance of HisGal against thermal degradation and inhibitory effects caused by the presence of sodium, potassium, magnesium, and calcium ions. Moreover, cobalt-based supports significantly reduced galactose inhibition and enhanced lactose affinity in skim milk systems. These findings highlight the versatility and biotechnological potential of iron-free cobalt- and nickel-based magnetic nanoparticles as efficient supports for enzyme immobilization, offering rapid and efficient recovery of immobilized β-galactosidase and contributing to the economic viability of these processes.

Graphical Abstract

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来源期刊
Catalysis Letters
Catalysis Letters 化学-物理化学
CiteScore
5.70
自引率
3.60%
发文量
327
审稿时长
1 months
期刊介绍: Catalysis Letters aim is the rapid publication of outstanding and high-impact original research articles in catalysis. The scope of the journal covers a broad range of topics in all fields of both applied and theoretical catalysis, including heterogeneous, homogeneous and biocatalysis. The high-quality original research articles published in Catalysis Letters are subject to rigorous peer review. Accepted papers are published online first and subsequently in print issues. All contributions must include a graphical abstract. Manuscripts should be written in English and the responsibility lies with the authors to ensure that they are grammatically and linguistically correct. Authors for whom English is not the working language are encouraged to consider using a professional language-editing service before submitting their manuscripts.
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