Support Enzyme Loading Influences the Effect of Aldehyde Dextran Modification on the Specificity of Immobilized Ficin for Large Proteins
It has been reported that the modification of immobilized glyoxyl–ficin with aldehyde dextran can promote steric hindrances that greatly reduce the activity of the immobilized protease against hemoglobin, while the protease still maintained a reasonable level of activity against casein. In this pape...
| Autores: | , , , |
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| Tipo de recurso: | artículo |
| Fecha de publicación: | 2024 |
| País: | España |
| Institución: | Universidad Complutense de Madrid (UCM) |
| Repositorio: | Docta Complutense |
| Idioma: | inglés |
| OAI Identifier: | oai:docta.ucm.es:20.500.14352/112286 |
| Acceso en línea: | https://hdl.handle.net/20.500.14352/112286 |
| Access Level: | acceso abierto |
| Palabra clave: | 577.1 577.152.34 577.2 544.47 Steric hindrances Size specificity Tuning enzyme specificity Enzyme loading Immobilized proteases Bioquímica (Biología) Biología molecular (Biología) 2403 Bioquímica 2302.09 Enzimología 2210.01 Catálisis 2415 Biología Molecular |
| Sumario: | It has been reported that the modification of immobilized glyoxyl–ficin with aldehyde dextran can promote steric hindrances that greatly reduce the activity of the immobilized protease against hemoglobin, while the protease still maintained a reasonable level of activity against casein. In this paper, we studied if this effect may be different depending on the amount of ficin loaded on the support. For this purpose, both the moderately loaded and the overloaded glyoxyl–ficin biocatalysts were prepared and modified with aldehyde dextran. While the moderately loaded biocatalyst had a significantly reduced activity, mainly against hemoglobin, the activity of the overloaded biocatalyst was almost maintained. This suggests that aldehyde dextran was able to modify areas of the moderately loaded enzyme that were not available when the enzyme was overloaded. This modification promoted a significant increase in biocatalyst stability for both biocatalysts, but the stability was higher for the overloaded biocatalyst (perhaps due to a combination of inter- and intramolecular crosslinking). |
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