Center for Research and Development of Fine Chemicals, Guizhou University, Guiyang, 550025, People's Republic of China.
Key Laboratory of Agricultural and Animal Products Store & Processing of Guizhou Province, Guizhou University, Guiyang, 550025, People's Republic of China.
Appl Microbiol Biotechnol. 2024 Feb 24;108(1):233. doi: 10.1007/s00253-024-13071-z.
Enzyme immobilized on magnetic nanomaterials is a promising biocatalyst with efficient recovery under applied magnets. In this study, a recombinant extracellular lipase from Aspergillus niger GZUF36 (PEXANL1) expressed in Pichia pastoris GS115 was immobilized on ionic liquid-modified magnetic nano ferric oxide (FeO@SiO@ILs) via electrostatic and hydrophobic interaction. The morphology, structure, and properties of FeO@SiO@ILs and immobilized PEXANL1 were characterized by scanning electron microscopy, Fourier transform infrared spectroscopy, x-ray diffraction, vibration sample magnetometer, and zeta potential analysis. Under optimized conditions, the immobilization efficiency and activity recovery of immobilized PEXANL1 were 52 ± 2% and 122 ± 2%, respectively. The enzymatic properties of immobilized PEXANL1 were also investigated. The results showed that immobilized PEXANL1 achieved the maximum activity at pH 5.0 and 45 °C, and the lipolytic activity of immobilized PEXANL1 was more than twice that of PEXANL1. Compared to PEXANL1, immobilized PEXANL1 exhibited enhanced tolerance to temperature, metal ions, surfactants, and organic solvents. The operation stability experiments revealed that immobilized PEXANL1 maintained 86 ± 3% of its activity after 6 reaction cycles. The enhanced catalytic performance in enzyme immobilization on FeO@SiO@ILs made nanobiocatalysts a compelling choice for bio-industrial applications. Furthermore, FeO@SiO@ILs could also benefit various industrial enzymes and their practical uses. KEY POINTS: • Immobilized PEXANL1 was confirmed by SEM, FT-IR, and XRD. • The specific activity of immobilized PEXANL1 was more than twice that of PEXANL1. • Immobilized PEXANL1 had improved properties with good operational stability.
固定在磁性纳米材料上的酶是一种很有前途的生物催化剂，在应用磁场时可以高效回收。在这项研究中，通过静电和疏水相互作用，将黑曲霉 GZUF36（PEXANL1）在巴斯德毕赤酵母 GS115 中表达的重组细胞外脂肪酶固定在离子液体修饰的磁性纳米氧化铁（FeO@SiO@ILs）上。通过扫描电子显微镜、傅里叶变换红外光谱、X 射线衍射、振动样品磁强计和 Zeta 电位分析对 FeO@SiO@ILs 和固定化 PEXANL1 的形貌、结构和性能进行了表征。在优化条件下，固定化 PEXANL1 的固定化效率和酶活回收率分别为 52±2%和 122±2%。还研究了固定化 PEXANL1 的酶学性质。结果表明，固定化 PEXANL1 在 pH5.0 和 45°C 时达到最大活性，且固定化 PEXANL1 的脂肪酶活力是 PEXANL1 的两倍多。与 PEXANL1 相比，固定化 PEXANL1 对温度、金属离子、表面活性剂和有机溶剂具有更高的耐受性。操作稳定性实验表明，固定化 PEXANL1 在 6 次反应循环后仍保持 86±3%的活性。FeO@SiO@ILs 上固定化 PEXANL1 提高了催化性能，使纳米生物催化剂成为生物工业应用的理想选择。此外，FeO@SiO@ILs 还可以应用于各种工业酶及其实际应用。关键点： • 通过 SEM、FT-IR 和 XRD 证实了固定化 PEXANL1。 • 固定化 PEXANL1 的比酶活是 PEXANL1 的两倍多。 • 固定化 PEXANL1 具有改善的性能，具有良好的操作稳定性。
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