Aversa Isabella F S, Cavalcanti Marcello H S, Pereira Thalles M, A de Castro Alexandre, Tavano Olga L, Coelho Yara L, da Silva Luis H M, Gorup Luiz F, Ramalho Teodorico C, Virtuoso Luciano S
Colloid Chemistry Group, Chemistry Institute, Federal University of Alfenas (UNIFAL-MG), 700 Gabriel Monteiro da Silva street, Alfenas, MG 37130-000 , Brazil.
Department of Chemistry, Federal University of Lavras, Lavras, MG 37200-000, Brazil.
ACS Omega. 2025 Jun 2;10(22):22970-22983. doi: 10.1021/acsomega.5c00797. eCollection 2025 Jun 10.
This study explores the immobilization of porcine trypsin (PT) on superparamagnetic iron oxide nanoparticles (SPIONs) via adsorption, with a focus on both immobilization conditions and a comprehensive energetic evaluationan aspect often neglected in the literature. Isothermal titration calorimetry (ITC) revealed that interactions at pH 8.0 are energetically favorable, with a Δ° of -43.0 kJ mol, suggesting robust noncovalent interactions. PM6 calculations confirmed the stability of the adsorption. The resulting nanobiocatalyst showed over 75% activity recovery at pH 8.0 and retained around 40% activity after four reuse cycles, demonstrating its efficiency and robustness. The detailed energetic analysis provides critical insights for optimizing immobilization processes, impacting cost and technical feasibility, and advancing the understanding of enzyme-support interactions for scalable applications in biocatalysis.
本研究通过吸附法探索了猪胰蛋白酶（PT）在超顺磁性氧化铁纳米颗粒（SPIONs）上的固定化，重点关注固定化条件和全面的能量评估——这是文献中经常被忽视的一个方面。等温滴定量热法（ITC）表明，在pH 8.0时的相互作用在能量上是有利的，Δ°为 -43.0 kJ/mol，表明存在强大的非共价相互作用。PM6计算证实了吸附的稳定性。所得的纳米生物催化剂在pH 8.0时显示出超过75%的活性回收率，并且在四个重复使用循环后保留了约40%的活性，证明了其效率和稳健性。详细的能量分析为优化固定化过程提供了关键见解，影响成本和技术可行性，并推进了对酶-载体相互作用的理解，以实现生物催化中可扩展应用。
