%0 Journal Article
%A Bernal Zuloaga, Claudia Patricia
%A Marciello, Marzia
%A Mesa Cadavid, Mónica 
%A Sierra, María Ligia 
%A Fernández-Lorente, Gloria 
%A Mateo González, César 
%A Guisan Seijas, José Manuel 
%T Immobilisation and stabilisation of β-galactosidase from Kluyveromyces lactis using a glyoxyl support
%D 2013
%@ 0958-6946
%U https://hdl.handle.net/20.500.14352/100883
%X 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.
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