The origin of ultraslow component of solvation observed in an aqueous protein solution is studied by femtosecond up-conversion. It has been observed that solvation dynamics in hen egg lysozyme and lysozyme- cetyltrimethylammonium bromide (CTAB) aggregate exhibits a nearly twofold slowing down when the solvent H 2O is replaced by D 2O. The deuterium isotope effect suggests that water is the main polar species responsible for the observed ultrafast solvation dynamics in the aqueous protein solution.