Arginine ethylester prevents thermal inactivation and aggregation of lysozyme.
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.
Shiraki
Kentaro
K
School of Materials Science, Japan Advanced Institute of Science and Technology (JAIST), Tatsunokuchi, Japan.
Kudou
Motonori
M
Nishikori
Shingo
S
Kitagawa
Harue
H
Imanaka
Tadayuki
T
Takagi
Masahiro
M
D000818:Animals; D001120:Arginine / Q000031:analogs & derivatives / Q000494:pharmacology*; D002152:Calorimetry, Differential Scanning; D002645:Chickens; D002942:Circular Dichroism; D004795:Enzyme Stability / Q000187:drug effects; D005260:Female; D006863:Hydrogen-Ion Concentration; D009113:Muramidase / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding / Q000187:drug effects; D011489:Protein Denaturation / Q000187:drug effects; D017510:Protein Folding; D055672:Static Electricity; D013696:Temperature
D001120:Arginine; C489258:arginine ethyl ester; C421864:hen egg lysozyme; D009113:Muramidase