RT Journal Article
T1 Vinyl sulfone-amino-alkyl supports: heterofunctional matrixes to prevent enzyme release and stabilize lipases via covalent immobilization
A1 Abellanas Pérez, Pedro
A1 de Andrades, Diandra
A1 Alcántara León, Andrés Rafael
A1 Rocha Martín, Javier
A1 Polizeli, Maria de Lourdes Teixeira de Moraes
A1 Fernandez Lafuente, Roberto
AB New trifunctional supports were prepared (amino-octyl-vinyl sulfone (VS)- and amino-hexyl-VS-agarose) and compared to octyl-VS-agarose. They were utilized to immobilize the lipases A and B from Candida antarctica (CALA and CALB). After incubation to generate some enzyme-support bonds and blocking with different nucleophiles, SDS-PAGE analyses showed that all enzyme molecules become covalently immobilized on the support. In all VS biocatalysts, the blocking reagent presented a great effect in the properties of enzymes. The best blocking agents promoted a significant enzyme stabilization compared to the enzyme stability using the amino-alkyl-agarose supports, higher than that using octyl-VS-agarose supports, although these remained the most stable ones in most cases, as the octyl-biocatalysts were significantly more stable than the enzyme immobilized on amino-alkyl-support. Enzyme activities and specificities could be also greatly tuned by the immobilization in the new trifunctional supports, with enzyme activities in many instances enhancing that of the best non-covalently immobilized enzyme. That way, the results on this paper show that the properties of the enzymes when immobilized on these new trifunctional supports may be significantly tuned by the nature of the acyl chain in the support and the nature of the reagent used to block the reactivity of the remaining VS groups.
PB Elsevier
SN 0141-8130
YR 2025
FD 2025-04
LK https://hdl.handle.net/20.500.14352/121053
UL https://hdl.handle.net/20.500.14352/121053
LA eng
NO Abellanas-Perez P, De Andrades D, Alcantara AR, Rocha-Martin J, Polizeli MDLTDM, Fernandez-Lafuente R. Vinyl sulfone-amino-alkyl supports: heterofunctional matrixes to prevent enzyme release and stabilize lipases via covalent immobilization. International Journal of Biological Macromolecules 2025;310:143305. https://doi.org/10.1016/j.ijbiomac.2025.143305.
NO Acknowledgements:We gratefully recognize the financial support from Ministerio de Ciencia e Innovación and Agencia Estatal de Investigación (Spanish Government) (PID2022-136535OB-I00). JR-M recognize the support from Grant CNS2022-135135 funded by MICIU/AEI/10.13039/501100011033 and European Union NextGenerationEU/PRTR and Grant PID2022-139209OB-C22 funded by MICIU/AEI/10.13039/501100011033 and ERDF/EU. The authors gratefully acknowledge FAPESP (São Paulo Research Foundation) by research scholarship to DA (Grant No: 2020/15510-8 and 2023/01338-7).
NO European Commission
NO Ministerio de Ciencia e Innovación (España)
NO Agencia Estatal de Investigación (España)
NO Ministerio de Ciencia, Innovación y Universidades (España)
NO Fundação de Amparo à Pesquisa do Estado de São Paulo (Brazil)
DS Docta Complutense
RD 8 jun 2025