Hydrophobic Covalent Organic Frameworks as a Platform for Instantaneous and High‐Capacity Immobilization of Diutina (Candida) rugosa Lipase: A Simple Strategy to Boost Enzyme Activity
- 1Instituto de Química Universidade Federal do Rio de Janeiro Rio de Janeiro Brazil
- 2Programa de Pós‐Graduação em Ciência e Engenharia de Materiais (PPGMAT) Universidade de Caxias do Sul (UCS) Caxias do Sul Rio Grande do Sul (RS) Brazil
- 3Departamento de Tecnologia LBIOP – Laboratório de Biotecnologia de Produtos Naturais e Sintéticos Instituto de Biotecnologia Universidade de Caxias do Sul Caxias do Sul Brazil
Abstract
Covalent Organic Frameworks (COFs) are emerging as promising platforms for enzyme immobilization; however, the impact of their structural and chemical properties on adsorption and enzymatic activity remains underexplored. Here, Diutina rugosa lipase (DrL) was immobilized on four COFs (RIO‐12, RIO‐13, RIO‐54, and RIO‐55) synthesized from simple, commercially available precursors. The effects of COF chemical composition and textural properties on adsorption dynamics and catalytic performance were evaluated. Immobilization occurred almost instantaneously, reaching completion in less than 10 s regardless of the COF used, with loading efficiencies of 99.8%–99.9%, protein binding capacities of approximately 44 mg g−1 of support, and enzyme leaching below 0.3% per washing cycle for all composites. Our results show that fully organic COF surfaces, rich in aromatic and nitrogen‐containing functional groups, exhibit a strong affinity for lipases, enabling rapid immobilization primarily driven by hydrophobic interactions, whereas pore size and surface area play a secondary role. In contrast, enzymatic activity was strongly influenced by surface area, likely through a positive partition effect that increases the local substrate concentration near the enzyme. Notably, RIO‐12 exhibited a remarkable enhancement in activity, achieving a specific activity 14.8‐fold higher than that of the free enzyme (408.5 vs. 27.7 U mg−1).
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BibTeX
@article{dobler2026hydrophobic,
title = {{Hydrophobic Covalent Organic Frameworks as a Platform for Instantaneous and High‐Capacity Immobilization of Diutina (Candida) rugosa Lipase: A Simple Strategy to Boost Enzyme Activity}},
author = {Leticia Dobler and Mirian Lima de Almeida Lippi and Luiz Octávio Mateus Nogueira and Davi Forastieri Tostes and Alexandre da Silva França and Fábio Junior Ferreira da Silva Henrique and Leandro Sodré de Abreu and Gabriel Almeida Mendonça da Silva and Cesar Aguzzoli and Sidnei Moura e Silva and Rodrigo O. M. A. de Souza and Rodrigo Volcan Almeida and Pierre Mothé Esteves and Raoni Schroeder Borges Gonçalves},
journal = {Chempluschem},
year = {2026},
month = nov,
doi = {10.1002/cplu.70284},
url = {https://doi.org/10.1002/cplu.70284},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - Hydrophobic Covalent Organic Frameworks as a Platform for Instantaneous and High‐Capacity Immobilization of Diutina (Candida) rugosa Lipase: A Simple Strategy to Boost Enzyme Activity
AU - Leticia Dobler
AU - Mirian Lima de Almeida Lippi
AU - Luiz Octávio Mateus Nogueira
AU - Davi Forastieri Tostes
AU - Alexandre da Silva França
AU - Fábio Junior Ferreira da Silva Henrique
AU - Leandro Sodré de Abreu
AU - Gabriel Almeida Mendonça da Silva
AU - Cesar Aguzzoli
AU - Sidnei Moura e Silva
AU - Rodrigo O. M. A. de Souza
AU - Rodrigo Volcan Almeida
AU - Pierre Mothé Esteves
AU - Raoni Schroeder Borges Gonçalves
PY - 2026
DA - 2026/11/04
JO - Chempluschem
DO - 10.1002/cplu.70284
UR - https://doi.org/10.1002/cplu.70284
AB - Covalent Organic Frameworks (COFs) are emerging as promising platforms for enzyme immobilization; however, the impact of their structural and chemical properties on adsorption and enzymatic activity remains underexplored. Here, Diutina rugosa lipase (DrL) was immobilized on four COFs (RIO‐12, RIO‐13, RIO‐54, and RIO‐55) synthesized from simple, commercially available precursors. The effects of COF chemical composition and textural properties on adsorption dynamics and catalytic performance were evaluated. Immobilization occurred almost instantaneously, reaching completion in less than 10 s regardless of the COF used, with loading efficiencies of 99.8%–99.9%, protein binding capacities of approximately 44 mg g−1 of support, and enzyme leaching below 0.3% per washing cycle for all composites. Our results show that fully organic COF surfaces, rich in aromatic and nitrogen‐containing functional groups, exhibit a strong affinity for lipases, enabling rapid immobilization primarily driven by hydrophobic interactions, whereas pore size and surface area play a secondary role. In contrast, enzymatic activity was strongly influenced by surface area, likely through a positive partition effect that increases the local substrate concentration near the enzyme. Notably, RIO‐12 exhibited a remarkable enhancement in activity, achieving a specific activity 14.8‐fold higher than that of the free enzyme (408.5 vs. 27.7 U mg−1).
SN - 2192-6506
ER -