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KMID : 0604520000260010107
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Journal of the Society of Cosmetic Scientists of Korea
2000 Volume.26 No. 1 p.107 ~ p.124
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Purification and Identification of protease from Bacillus sp. HB-5 and its application of cosmetic product
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이범천/Lee, Bum-Chun
윤은정/이동환/표형배/Yoon, Eun-Jeong/Lee, Dong-Hwan/Pyo, Hyeong-Bae
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Abstract
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A bacterial strain No. HB-5, which was capable of producing a protease in the culture conditions, was isolated from the soil. The protease was purified from cultural filtrate of Aacillus sp. HB-5 by membrane ultrafiltration and DEAE-cellulose chromatography, gel filtration on Sephadex G-100. The molecular weight was estimated to be 60Kda. The optimal pH and temperature for the activity of the purified protease pH were 11 and 50℃, respectively. The enzyme was stable within a PH range 8-12 and up to 60℃. The enzyme activity was highly inhibited by PMSF at 1mM. The proteolytic actions of protease and papain on human epidermis keratins, which are major protein impurities on the skin, were compared. The bacterial protease degraded more effectively than papain. Product containing 2% protease exhibited 21% increase on the skin coloration index. These results suggest that cosmetic product containing protease produced by Bacillus sp. HB-5 could remove the adherent keratin layer and then make a softer skin.
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