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Immobilization of lactoperoxidase on ZnO nanoparticles with improved stability
Biotechnology Letters ( IF 2.7 ) Pub Date : 2020-02-04 , DOI: 10.1007/s10529-020-02828-x
Mehrnaz Movahedi 1 , Seyed Ziyae Aldin Samsam Shariat 2 , Habibollah Nazem 1 , Mehrdad Movahedi 3
Affiliation  

Objectives The study aimed to develop a facile and effectual method to enhance the stability of lactoperoxidase (LPO) by immobilizing it on ZnO Nanoparticles (ZnO NPs). Results The successful immobilization of LPO on ZnO NPs was confirmed by using Fourier transform infrared spectroscopy (FT-IR) and field emission scanning electron microscopy (FE-SEM). The K m values of free LPO and LPO immobilized on ZnO were 53.19, 89.28 mM and their V max values were 0.629, 0.46 µmol/mL min, respectively. The overall results showed that the stability of the immobilized LPO was significantly improved compared to free LPO. The LPO immobilized on ZnO (LPO–ZnO) retained 18% of the initial activity within 30 days at 25 °C whereas the free enzyme lost its activity after 7 days at the same temperature. Moreover, evaluation of the thermal stability of LPO at 75 °C determined the conservation of 12% of the initial activity of LPO in the LPO–ZnO sample after 60 min whereas the free enzyme lost its activity after 5 min. Conclusions According to the present results, ZnO nanoparticles are suitable for the immobilization of LPO.

中文翻译:

将乳过氧化物酶固定在具有更高稳定性的 ZnO 纳米颗粒上

目的 本研究旨在开发一种简便有效的方法,通过将乳过氧化物酶 (LPO) 固定在 ZnO 纳米颗粒 (ZnO NPs) 上来提高其稳定性。结果通过傅里叶变换红外光谱 (FT-IR) 和场发射扫描电子显微镜 (FE-SEM) 证实了 LPO 在 ZnO NPs 上的成功固定。游离 LPO 和固定在 ZnO 上的 LPO 的 K m 值分别为 53.19、89.28 mM 和它们的 V max 值分别为 0.629、0.46 µmol/mL min。总体结果表明,与游离 LPO 相比,固定化 LPO 的稳定性显着提高。固定在 ZnO 上的 LPO(LPO-ZnO)在 25°C 下 30 天内保留了初始活性的 18%,而游离酶在相同温度下 7 天后失去活性。而且,对 LPO 在 75 °C 下的热稳定性的评估确定了 60 分钟后 LPO-ZnO 样品中 LPO 初始活性的 12% 的保守性,而游离酶在 5 分钟后失去了其活性。结论 根据目前的结果,ZnO 纳米颗粒适用于 LPO 的固定。
更新日期:2020-02-04
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