The Protease as a Cleansing Agent and Its Stabilization by Chemical Modification.

Abstract

The effect of protease as a cleansing agent and the improvement of protease stability by chemical modification with polyethylene glycol derivatives were studied. The proteolytic actions of Bioprase and papain on keratins and sweat proteins, which are major proteinic impurities on the skin, were compared. Bioprase degraded both more effectively than papain. Although Bioprase possesses potential usefulness as a cosmetic material, it has a defect: low staility in a system containing water. This defect prevents the application of Bioprase to various preparations except for powder-type preparations. To improve the stability of the native Bioprase, it was chemically modified with copolymers of α-allyl-ω-methoxy polyoxyethylene and maleic anhydride. The stability of Bioprase was extremely improved by the modification. The modified Bioprase was further stabilized by adding such polyols as 1, 3-butylene glycol, glycerin, and propylene glycol. Some nonionic surfactants did not decrease the stability of the modified Bioprase. This method for stabilization allows the application of enzyme to various preparations. By continual use of a cleansing preparation containing the modified Bioprase, skin conditions improved.