Concentration Of Egg White Lysozyme In The Serum Of Healthy Subjects After Oral Administration

Egg white lysozyme preparation ER0068 (Neuzym (R); Eisai, Tokyo, Japan) is widely used clinically, but its pharmacokinetic properties at clinically relevant doses have not been studied. In this study, a high sensitivity two-site enzyme immunoassay was used to determine the pharmacokinetic properties of egg white lysozyme after oral administration of two doses in a clinical setting, with particular attention to the effects of food intake.

2. A total of 22 healthy male subjects aged 20 to 45 participated in the study. All subjects were screened for egg white allergy and nonspecific lysozyme inhibitors in serum. Subjects receiving 90 mg of ER 0068 after a rapid overnight reached a maximum serum concentration of 1700 pg / mL within 1 hour compared to undetectable levels in untreated controls. In a second experiment, subjects received 30 and 90 mg of ER0068 after an overnight fast and received 90 mg in the fasted state, showing maximum serum levels of 37, 360 and 49 pg / mL, respectively. After 48 hours, serum albumen lysozyme concentration returned to undetectable levels

We conclude that clinically relevant concentration of egg white lysozyme is highly absorbed despite its high molecular weight. However, food intake greatly reduces enzyme intake

Typical data on protein solids distribution, lysozyme yield and activity of the resulting formulation are shown in Table II. These data indicate that up to 90% of the lysozyme present in the egg white can be obtained at this concentration 35 to 40 times the concentration of the original egg white solid. Within the margin of error of the assay method, the activity of the material is constant from formulation to formulation. The concentration of the active substance contained in the eluate at pH 5.0 can be achieved in various ways. The active substance was precipitated by adding ammonium sulfate at a concentration of 2.6 M and collected by centrifugation or filtration. The precipitate readily dissolves in distilled water and the solution can be removed by dialing. The solution is dried in the frozen state to obtain a white solid.

Earlier chemistry efforts focused only on the active ingredients of egg whites. Available evidence is provided primarily by Abraham (2), indicating that lysozyme is a basic protein with a molecular weight close to 18,000. Abraham reported that it is stable when heated in acidic solution but very thermally unstable in alkali. Acetone, diethyl ether and ethanol precipitated the active substance from the aqueous solution without destroying it. The latter property is the basis of the preparation method designed by Roberts (3) and Meyer et al. (4) In these methods, initial purification is obtained by inactivating the majority of egg albumin by selective acetone denaturation in the alkaline reaction of natural protein. Meyer et al. (4) The precipitated protein was first extracted with a mixed solution of alcohol and acetic acid aqueous solution. Lysine precipitation with lysine