Design of β-galactosidase/silica biocatalysts: Impact of the enzyme properties and immobilization pathways on their catalytic performance
Article first published online: 31 JUL 2013
© 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Engineering in Life Sciences
Volume 14, Issue 1, pages 85–94, January 2014
How to Cite
Bernal, C., Sierra, L. and Mesa, M. (2014), Design of β-galactosidase/silica biocatalysts: Impact of the enzyme properties and immobilization pathways on their catalytic performance. Eng. Life Sci., 14: 85–94. doi: 10.1002/elsc.201300001
- Issue published online: 16 JAN 2014
- Article first published online: 31 JUL 2013
- Accepted manuscript online: 5 JUN 2013 01:39AM EST
- Manuscript Accepted: 23 APR 2013
- Manuscript Revised: 1 MAR 2013
- Manuscript Received: 2 JAN 2013
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Figure S1. Characteristics for the synthesized silica: (A) BJH pore size distribution for the main cavities for the bare (▪) and modified-silica SGx6.0 ( ). (B, C) SEM micrographs for the bare silica (S) before (B) and after (C) be submitted to the immobilization conditions.
Figure S2. Solid state 29Si NMR spectrum for the silica modified by using GPTMS (S-Gx6.0 material)
Figure S3. Isoelectric point for pure silica, B. circulans (square), A oryzae (circles) and K. lactis (triangle) -galactosidades and silica (continues line).
Figure S4. Thermal stability at 55°C and pH 4.5 for Aspergillus oryzae -galactosidase before (▪) and after (○) amination process.
Figure S5. SDS-PAGE analysis of β-galactosidase from K. lactis (free or immobilized in glyoxyl-activated agarose support). Lane 1: molecular weight markers; lane 2: free β- galactosidase; lane 3: β-galactosidase immobilized in glyoxyl-activated agarose support
Figure S6. Lineweaver-Burk plot for β-galactosidase from B. circulans: free (▪), immbolized in glyoxyl-activated silica (▲, Bc-SGx1.0 ) and agarose (Δ, Bc-AGx)
Table S1. Some characteristics for the -galactosidades studied in this work
Table S2. Porous characteristics and aldehyde content for the different supports
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