Lysine ionic properties

The Effect on Physical Properties. The most effective reaction of MTG is the crosslinking through 6-(y-Glu)Lys bonds (Fig. 1-b). When e-amino groups of lysine residues act as acyl acceptors, e-(y-Glu)Lys crosslinks are formed. The crosslinking reaction may be both intermolecular and intramolecular and causes significant physical property changes in protein-rich foods. The e-(y-Glu)Lys bonds are covalent bonds which are stable unlike ionic bonds and hydrophobic bonds. Therefore, even the few e-(y-Glu)Lys bonds in foods have a profound effect on the physical properties. 

Unlike enantiomers, diastereomers have different solubilities in an achiral environment. Many chiral counterions, such as arginine and lysine, are commonly used to prepare salts of an ionic drug in order to improve its pharmaceutically relevant properties. However, when the drug is chiral, a chiral counterion should be used with caution. If the drug or the counterion is racemic, diastereomeric salts will be formed, constituting a heterogeneous system. Because the solubilities of diastereomers differ, a diastereomeric mixture of chiral salts is undesirable in a formulation. 

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