RT Journal Article
T1 The Effects of Buffer Nature on Immobilized Lipase Stability Depend on Enzyme Support Loading
A1 Abellanas Pérez, Pedro
A1 Carballares Navarro, Diego
A1 Rocha Martín, Javier
A1 Fernandez Lafuente, Roberto
AB 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.
PB MDPI
SN 2073-4344
YR 2024
FD 2024-01-26
LK https://hdl.handle.net/20.500.14352/119670
UL https://hdl.handle.net/20.500.14352/119670
LA eng
NO 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
NO Ministerio de Ciencia e Innovación (España)
DS Docta Complutense
RD 8 jun 2026