Glyoxyl agarose: A fully inert and hydrophilic support for immobilization and high stabilization of proteins

By C. Mateo, J. Palomo, M. Fuentes, L. Betancor, V. Grazú, F. López‐Gallego, B. Pessela, A. Hidalgo, G. Fernandez-Lorente, R. Fernández-Lafuente and 1 more. 2006

380 citations recorded by the source corpus.

Subfields: Materials Chemistry, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/209ad7911109fbfdfa8964f770b6422ddc3ba007

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Materials Chemistry

1. R. Fernández-Lafuente
2. Á. Berenguer-Murcia
3. R. Rodrigues
4. C. Ortiz

In Molecular Biology

1. R. Fernández-Lafuente
2. C. Ortiz
3. Á. Berenguer-Murcia
4. O. Barbosa
5. R. Torres
6. R. Rodrigues

Citations in the corpus

• Biotechnological relevance of the lipase A from Candida antarctica (2021, background): “heterofunctional acyl-glyoxyl supports, where the enzymes are immobilized at pH 7 to prevent the direct covalent immobilization [175,238] and ensures the immobilization via”
• Strategies for the one-step immobilization-purification of enzymes as industrial biocatalysts. (2015, methodology): “, 2007a, 2007b) and glyoxyl groups (Mateo et al., 2006) have been utilized.”