Effect of amine length in the interference of the multipoint covalent immobilization of enzymes on glyoxyl agarose beads

Trypsin, chymotrypsin, penicillin G acylase and ficin extract have been stabilized by immobilization on glyoxyl agarose, adding different aliphatic compounds bearing a primary amine group during the immobilization: ethyl amine, butyl hexyl (at concentrations ranging from 0 to 20 mM) octyl (from 10 analyze their effects immobilized enzyme stability. As expected, presence of amines reduced intensity enzyme-support multipoint covalent attachment, therefore However, it is clear that this effect higher using for all enzymes (in some cases in mM was almost inactivated while reference kept over 50 % initial activity). This way, seems most important aminated came generation steric hindrances enzyme/support multi-reaction promoted ammines are interacting with aldehyde groups. In instances, just 1 enough greatly decrease The results suggested that, if composition unknown, eliminate small may be necessary maximize reaction.