Some special features of glyoxyl supports to immobilize proteins

By C. Mateo, O. Abián, M. Bernedo, E. Cuenca, M. Fuentes, G. Fernandez-Lorente, J. Palomo, V. Grazú, B. Pessela, Cecilia Giacomini and 6 more. 2005

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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”
Improvement of enzyme activity, stability and selectivity via immobilization techniques (2007, background): “10,000a [41] 60,000a [45] 8,000a [42] 7,000a [43] 1,000a [23] 150a [54] 1,000a [49] 100a [50] 1,000a [33] >5,000a [24] 150a [70] >3,000 [68] >100 [64] >100 [69] >50 [59] 60 [65] 500 [46] 10 [55]”
Glyoxyl agarose: A fully inert and hydrophilic support for immobilization and high stabilization of proteins (2006, background): “, proteins having several terinal amino groups, as, for example, some multimeric enzymes, ome proteolyzed proteins) to permit the first multipoint attachent [16].”
Strategies for the one-step immobilization-purification of enzymes as industrial biocatalysts. (2015, methodology): “Glyoxyl, as stated above, cannot immobilize monomeric proteins at neutral pH value (Mateo et al., 2005).”