Mukhopadhyay R P, Chandra A L
Department of Microbiology, Bose Institute, Calcutta, India.
Indian J Exp Biol. 1990 Jun;28(6):575-7.
Keratinase produced from Streptomyces Sp.A11 decomposed human hair, chicken feather, wool, silk and pure keratin extracted from human epidermis. Purification of the enzyme by DEAE-cellulose column chromatography resulted in 7.5-fold increase in activity relative to the activity of the culture filtrate. The enzyme was inducible, extracellular, homogeneous with a molecular weight of 49,000. The enzyme activity was inhibited by reduced glutathione, phenylmethyl sulphonyl fluoride and 2-mercaptoethanol.
链霉菌Sp.A11产生的角蛋白酶可分解人发、鸡毛、羊毛、丝绸以及从人表皮提取的纯角蛋白。通过DEAE-纤维素柱色谱法对该酶进行纯化后，其活性相对于培养滤液的活性提高了7.5倍。该酶是诱导型的、胞外酶，分子量为49,000，呈均一性。该酶的活性受到还原型谷胱甘肽、苯甲基磺酰氟和2-巯基乙醇的抑制。
