RT Journal Article
T1 Tuning almond lipase features by the buffer used during immobilization: The apparent biocatalysts stability depends on the immobilization and inactivation buffers and the substrate utilized
A1 Cherni, Oumaima
A1 Carballares, Diego
A1 Siar, El Hocine
A1 Abellanas-Pérez, Pedro
A1 Andrades, Diandra de
A1 Teixeira de Moraes Polizeli, Maria de Lourdes
A1 Rocha Martín, Javier
A1 Bahri, Sellema
A1 Fernández-Lafuente, Roberto
AB The lipase from Prunus dulcis almonds was inactivated under different conditions. At pH 5 and 9, enzyme stability remained similar under the different studied buffers. However, when the inactivation was performed at pH 7, there were some clear differences on enzyme stability depending on the buffer used. The enzyme was more stable in Gly than when Tris was employed for inactivation. Then, the enzyme was immobilized on methacrylate beads coated with octadecyl groups at pH 7 in the presence of Gly, Tris, phosphate and HEPES. Its activity was assayed versus triacetin and S-methyl mandelate. The biocatalyst prepared in phosphate was more active versus S-methyl mandelate, while the other ones were more active versus triacetin. The immobilized enzyme stability at pH 7 depends on the buffer used for enzyme immobilization. The buffer used in the inactivation and the substrate used determined the activity. For example, glycine was the buffer that promoted the lowest or the highest stabilities depending on the substrate used to quantify the activities.
PB Elsevier
SN 0168-1656
YR 2024
FD 2024-08
LK https://hdl.handle.net/20.500.14352/118722
UL https://hdl.handle.net/20.500.14352/118722
LA eng
NO Cherni, O., Carballares, D., Siar, E.H., Abellanas-Perez, P., de Andrades, D., de Lourdes Teixeira de Moraes Polizeli, M., ... & Fernandez-Lafuente, R. (2024). Tuning almond lipase features by the buffer used during immobilization: The apparent biocatalysts stability depends on the immobilization and inactivation buffers and the substrate utilized. Journal of Biotechnology. https://doi.org/10.1016/j.jbiotec.2024.06.009
NO We gratefully recognize the financial support from Ministerio de Ciencia e Innovación and Agencia Estatal de Investigación (Spanish Government) (PID2022-136535OB-I00). Oumaima Cherni thanks the Tunisian Ministry of Higher Education and Scientific Research for her fellowship to perform her stay at ICP-CSIC. The authors gratefully acknowledge FAPESP (São Paulo Research Foundation) by research scholarship to DA (Grant No: 2023/01338-7). The help and suggestions from Dr. Ángel Berenguer (Departamento de Química Inorgánica, Universidad de Alicante) are gratefully recognized.
NO Ministerio de Ciencia e Innovación (España)
NO Agencia Estatal de Investigación (España)
NO Tunisian Ministry of Higher Education and Scientific Research
NO FAPESP (São Paulo Research Foundation)
DS Docta Complutense
RD 7 abr 2025