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在金属化聚合物纳米颗粒上L-asparaginase的固定和基于SPR的结合特征

Kübra Kaya¹, Samir Abbas Ali Noma¹, Monireh Bakhshpour-Yücel¹

¹Bursa Uludag University, Faculty of Arts and Science, Department of Chemistry, 16059 Gorukle, Bursa, Turkey.

International journal of biological macromolecules

|September 1, 2025

概括

聚合物纳米颗粒有效地固定L-asparaginase (L-ASNase),提高了酶的稳定性,活性和可重复使用性. 这种固定能提高制药和工业应用的催化性能.

科学领域:

生物材料科学
酶固定化
纳米技术

背景情况:

在癌症治疗中,L-asparaginase (L-ASNase) 是至关重要的,但其稳定性有限.
在纳米载体上酶固定可以克服稳定性和可重复使用性限制.

研究的目的:

合成和表征聚二乙基甲酸-N-甲基-L) -胺甲基-Cu2+) [PHMCu2+]纳米粒子.
在这些PHMCu2+纳米粒子上固定L-asparaginase.
评估L-ASNase的增强特性,以了解其潜在的应用.

主要方法:

用于纳米粒子合成的乳液聚合.
使用SEM-EDX,TEM,FTIR和Zeta潜力的表征.
表面等离子共振 (SPR) 用于结合亲和度分析.
在各种条件下进行酶活性测定和稳定性研究.

主要成果:

PHMCu2+纳米粒子成功地固定了L-ASNase,产量高 (86.4%) 和效率高 (85.1%).
固定L-ASNase显示了最佳pH值的变化为7.0和温度的变化为50°C.
观察到对蛋白质溶解的增强稳定性,提高可重复使用性 (在10个循环后具有60%的活性),以及对变性条件的更好的耐受性.
通过Langmuir模型,SPR证实了高结合亲和度 (KD=0. 016 IU/ ml).

结论:

PHMCu2+纳米粒子作为L-ASNase固定化的有效载体.
固定可显著提高酶的催化活性,稳定性和可重复使用性.
开发的系统有望用于需要强大的L-ASNase的制药和工业应用.

关键词:

生物催化剂的稳定性酶固定化在IMAC纳米颗粒一个L-酸蛋白酶耐药性提供治疗性酶

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