RT Journal Article
T1 Effect of the support alkyl chain nature in the functional properties of the immobilized lipases
A1 De Andrades, Diandra
A1 Abellanas Perez, Pedro
A1 Rocha Martín, Javier
A1 Lopez Gallego, Fernando
A1 Alcántara León, Andrés Rafael
A1 Polizeli, Maria de Lourdes Teixeira de Moraes
A1 Fernandez Lafuente, Roberto
AB Supports coated with amino-hexyl and amino octyl have been prepared from glyoxyl agarose beads and compared in their performance with octyl-agarose to immobilize lipases A and B from Candida antarctica (CALA and CALB). Immobilization courses were similar using all supports, but enzyme release was more difficult using the amino-alkyl supports suggesting a mixed interfacial activation/ionic exchange immobilization. The enzyme activity and specificity (using p-nitrophenyl propionate, triacetin and both isomers of methyl mandelate) greatly depended on the support. In many instances the enzymes immobilized on the new supports offered higher activities and enantiospecificity in the hydrolysis of both enantiomers of methyl mandelate (mainly using CALB). This was coupled to a lower enzyme stability using the new supports, even in the presence of high ionic strength, suggesting that the amphipathic could be responsible of the enzyme lower stability. Using CALB, it was possible to detect a higher exposition of the enzyme Trp groups to the medium by florescence spectra after its immobilization on the amino-alkyl-supports, correlating to the higher activity and lower stability results.
PB Elsevier
SN 0141-0229
YR 2025
FD 2025
LK https://hdl.handle.net/20.500.14352/118579
UL https://hdl.handle.net/20.500.14352/118579
LA eng
NO De Andrades, D., Abellanas-Perez, P., Rocha-Martin, J., Lopez-Gallego, F., Alcántara, A. R., Polizeli, M. D. L. T. D. M., & Fernandez-Lafuente, R. (2025). Effect of the support alkyl chain nature in the functional properties of the immobilized lipases. Enzyme and Microbial Technology, 184, 110583. https://doi.org/10.1016/j.enzmictec.2025.110583
NO We gratefully recognize the financial support from Ministerio de Ciencia e Innovación and Agencia Estatal de Investigación (Spanish Government) (PID2022–136535OB-I00). JR-M recognizes 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 Ministerio de Ciencia e Innovación (España)
NO Ministerio de Ciencia, Innovación y Universidades (España)
NO European Commission
NO Fundação de Amparo à Pesquisa do Estado de São Paulo
DS Docta Complutense
RD 14 dic 2025