RT Journal Article
T1 The nature of the buffer alters the effects of the chemical modification on the stability of immobilized lipases
A1 Abellanas Perez, Pedro
A1 Carballares, Diego
A1 Rocha Martín, Javier
A1 Fernandez Lafuente, Roberto
AB The objective of this paper was to analyze whether an interaction between the effects of the buffer nature and chemical modification on enzyme stability exists. For this, the lipase B from Candida antarctica (CALB) and the lipase from Thermomyces lanuginosus (TLL) were immobilized on octyl agarose beads and modified with picryl sulfonic acid (TNBS) and ethylenediamine via the carbodiimide route. The obtained biocatalysts were them inactivated in different buffers (2-amino-2-(hydroxymethyl)propane-1,3-diol (Tris)-HCl, N-(2-hydroxyethyl)piperazine-N′-(2-ethanesulfonic acid) (HEPES) or phosphate). A significant interaction was found between the chemical modification of the enzyme surfaces and their stabilities in these different buffers. While phosphate was the buffer where the lowest enzyme stabilities were found for both unmodified immobilized enzymes, the differences on enzyme stabilities become much smaller after some chemical modifications. In many instances, chemical modification improves enzyme stability when using a buffer and was negative when using the other one (e.g., TNBS modification of TLL was positive using Tris-HCl or negative using the other buffers, amination of CALB decreased its stability when inactivated in Tris-HCl or HEPES while it almost had no effect in phosphate). Thus, clear co-interactions of the effects o
PB Elsevier
SN 1359-5113
YR 2023
FD 2023-08
LK https://hdl.handle.net/20.500.14352/121295
UL https://hdl.handle.net/20.500.14352/121295
LA eng
NO Abellanas-Perez P, Carballares D, Rocha-Martin J, Fernandez-Lafuente R. The nature of the buffer alters the effects of the chemical modification on the stability of immobilized lipases. Process Biochemistry 2023;133:20–7. https://doi.org/10.1016/j.procbio.2023.08.003.
NO Ministerio de Ciencia e Innovación (España)
NO Agencia Estatal de Investigación (España)
DS Docta Complutense
RD 7 jun 2026