2026-06-08T09:10:57Zhttps://docta.ucm.es/rest/oai/request
oai:docta.ucm.es:20.500.14352/1196702025-04-24T23:50:40Zcom_20.500.14352_14col_20.500.14352_15
Docta Complutense author Abellanas Pérez, Pedro author Carballares Navarro, Diego author Rocha Martín, Javier author Fernandez Lafuente, Roberto 2025-04-24T08:38:43Z 2025-04-24T08:38:43Z 2024-01-26 Abellanas-Perez, P., Carballares, D., Rocha-Martin, J., & Fernandez-Lafuente, R. (2024). The Effects of Buffer Nature on Immobilized Lipase Stability Depend on Enzyme Support Loading. Catalysts, 14(2). https://doi.org/10.3390/CATAL14020105 2073-4344 10.3390/catal14020105 https://hdl.handle.net/20.500.14352/119670 https://doi.org/10.3390/catal14020105 https://www.mdpi.com/2073-4344/14/2/105 The lipases from Thermomyces lanuginosus (TLL) and Candida antarctica (B) (CALB) were immobilized on octyl-agarose beads at 1 mg/g (a loading under the capacity of the support) and by overloading the support with the enzymes. These biocatalysts were compared in their stabilities in 10 mM of sodium phosphate, HEPES, and Tris-HCl at pH 7. Lowly loaded CALB was more stable than highly loaded CALB preparation, while with TLL this effect was smaller. Phosphate was very negative for the stability of the CALB biocatalyst and moderately negative using TLL at both loadings. The stability of the enzymes in HEPES and Tris-HCl presented a different response as a function of the enzyme loading (e.g., using lowly loaded CALB, the stabilities were similar in both buffers, but it was clearly smaller in HEPES using the highly loaded biocatalysts). Moreover, the specific activity of the immobilized enzymes versus p-nitrophenol butyrate, triacetin and R- or S-methyl mandelate depended on the buffer, enzyme loading, and interaction between them. In some cases, almost twice the expected activity could be obtained using highly loaded octyl-CALB, depending on the buffer. A co-interaction between the effects on enzyme activity and the specificity of support enzyme loading and buffer nature was detected. eng Attribution 4.0 International The Effects of Buffer Nature on Immobilized Lipase Stability Depend on Enzyme Support Loading journal article 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URL https://docta.ucm.es/bitstreams/dafbc7bd-b214-4390-a5d2-becba5d17f94/download File MD5 558a7080a64f1cb8ddfd185c4afb32a1 1806034 application/pdf The_effects_of_buffer_nature.pdf