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A novel keratinase from Chryseobacterium sp. strain kr6 was purified to homogeneity by (NH4)2SO4 precipitation, gel permeation on Sephadex G-100, and Q-Sepharose Fast Flow anion-exchange chromatography. The molecular weight of the purified enzyme was around 20 kDa. Kinetic and thermodynamic parameters for thermal inactivation were determined. The influence of Ca2+ and Mg2+ ions and purification degree...
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