muramidase and arginine-ethyl-ester

Arginine is a versatile additive to prevent protein aggregation. This paper shows that arginine ethylester (ArgEE) prevents heat-induced inactivation and aggregation of hen egg lysozyme more effectively than arginine or guanidine. The addition of ArgEE decreased the melting temperature of lysozyme. This data could be interpreted in terms of ArgEE binding to unfolded lysozyme, possibly through the ethylated carboxyl group, which leads to effective prevention of intermolecular interaction among aggregation-prone molecules. The data suggest that ArgEE could be used as an additive to prevent inactivation and aggregation of heat-labile proteins.

Topics: Animals; Arginine; Calorimetry, Differential Scanning; Chickens; Circular Dichroism; Enzyme Stability; Female; Hydrogen-Ion Concentration; Muramidase; Protein Binding; Protein Denaturation; Protein Folding; Static Electricity; Temperature