RT Journal Article
T1 Immobilisation and stabilisation of β-galactosidase from Kluyveromyces lactis using a glyoxyl support
A1 Bernal Zuloaga, Claudia Patricia
A1 Marciello, Marzia
A1 Mesa Cadavid, Mónica
A1 Sierra, María Ligia
A1 Fernández-Lorente, Gloria
A1 Mateo González, César
A1 Guisan Seijas, José Manuel
AB β-galactosidase from Kluyveromyces lactis was covalently immobilised on a Glyoxyl Sepharose (GS) support by multi-point attachment. The enzyme immobilisation process was very efficient; the supports immobilised almost all the protein responsible for the catalytic activity in a short period of time, retaining approximately 82% of the activity in the case of the optimal immobilised preparations. Stability of the GS derivatives varied as a function of enzyme-support incubation time. The optimal immobilised preparation was produced after 2 h of incubation with the support at alkaline pH. This derivative, obtained by multi-point covalent attachment, was 100-fold more stable at pH 7 and 50 °C than the cyanogen bromide Sepharose derivative obtained by a one-point covalent immobilisation method. Stabilisation was also observed under a wide range of experimental conditions. This method allowed the immobilisation of 9000 IU enzyme g−1 of support, resulting in highly active and stable derivatives suitable for industrial processes.
PB Elsevier
SN 0958-6946
YR 2013
FD 2013-02
LK https://hdl.handle.net/20.500.14352/100883
UL https://hdl.handle.net/20.500.14352/100883
LA eng
NO Bernal C, Marciello M, Mesa M, Sierra L, Fernandez-Lorente G, Mateo C, et al. Immobilisation and stabilisation of β-galactosidase from Kluyveromyces lactis using a glyoxyl support. International Dairy Journal 2013;28:76–82. https://doi.org/10.1016/j.idairyj.2012.08.009.
NO COLCIENCIAS
NO Municipio de Rionegro
NO Universidad de Antioquia (Colombia)
DS Docta Complutense
RD 8 abr 2025