Multi-Point Covalent Immobilization of Enzymes on Glyoxyl Agarose with Minimal Physico-Chemical Modification: Stabilization of Industrial Enzymes.

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ID: 100178
2020
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Abstract
Stabilization of enzymes via immobilization techniques is a valuable approach in order to convert a necessary protocol (immobilization) into a very interesting tool to improve key enzyme properties (stabilization). Multipoint covalent attachment of each immobilized enzyme molecule may promote a very interesting stabilizing effect. The relative distances among all enzyme residues involved in immobilization have to remain unaltered during any conformational change induced by any distorting agent. Amino groups are very interesting nucleophiles placed on protein surfaces. The immobilization of enzyme through the region having the highest amount of amino groups (Lys residues) is key for a successful stabilization. Glyoxyl groups are small aliphatic aldehydes that form very unstable Schiff's bases with amino groups, and they do not seem to be useful for enzyme immobilization at neutral pH. However, under alkaline conditions, glyoxyl supports are able to immobilize enzymes via a first multipoint covalent immobilization through the region having the highest amount of lysine groups. Activation of supports with a high surface density of glyoxyl groups and the performance of very intense enzyme-support multipoint covalent attachments are here described.
Reference Key
lpezgallego2020multipointmethods Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors López-Gallego, Fernando;Fernandez-Lorente, Gloria;Rocha-Martín, Javier;Bolivar, Juan M;Mateo, Cesar;Guisan, Jose M;
Journal methods in molecular biology (clifton, nj)
Year 2020
DOI
10.1007/978-1-0716-0215-7_5
URL
Keywords
enzyme stabilization over-stabilization of aminated enzymes variables that control stabilization

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