Immobilization of Porcine Trypsin in Superparamagnetic Nanoparticles: Enzyme Activity and Stability

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 evaluationan aspect often neglected in the literature. Isothermal titration calorimetry (ITC) revealed that interactions at pH 8.0 are energetically favorable, with a Δ<i>H</i>° of -43.0 kJ mol<sup>-1</sup>, 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.

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Publication Details

Journal
ACS Omega
Published
2025-06-02
DOI
https://doi.org/10.1021/acsomega.5c00797
Citations
2
Primary Topic
Protein Interaction Studies and Fluorescence Analysis
Type
article
Field-Weighted Citation Impact
1.61

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article

Immobilization of Porcine Trypsin in Superparamagnetic Nanoparticles: Enzyme Activity and Stability

Teodorico C. Ramalho, Luís Henrique Mendes da Silva, Luciano Sindra Virtuoso, Isabella Fernandes Souza Aversa et al.
2 citations
ACS Omega
Protein Interaction Studies and Fluorescence Analysis
1.61
article

Immobilization of Porcine Trypsin in Superparamagnetic Nanoparticles: Enzyme Activity and Stability

Teodorico C. Ramalho, Luís Henrique Mendes da Silva, Luciano Sindra Virtuoso, Isabella Fernandes Souza Aversa, Olga Luisa Tavano, Alexandre A. de Castro, Yara Luíza Coelho, Luiz Fernando Gorup, Thalles Maranesi Pereira, Marcello H. S. Cavalcanti
article en
2 citations

Abstract

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 evaluationan aspect often neglected in the literature. Isothermal titration calorimetry (ITC) revealed that interactions at pH 8.0 are energetically favorable, with a Δ<i>H</i>° of -43.0 kJ mol<sup>-1</sup>, 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.

ACS OmegaVol. 10(22)
Universidade Federal de Juiz de Fora (BR), Universidade Federal de Lavras (BR), Universidade Federal de Viçosa (BR), Universidade Federal de Alfenas (BR)
Coordenação de Aperfeiçoamento de Pessoal de Nível Superior, Conselho Nacional de Desenvolvimento Científico e Tecnológico, Fundação de Amparo à Pesquisa do Estado de Minas Gerais
Openalex Percentile: Top 17%
Protein Interaction Studies and Fluorescence Analysis
1.61
DOIOpen Access PDFOpenAlex
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