Description
Proteinase K, a broad-spectrum serine protease, is first extracted and purified from Engyodontium album. It is named Proteinase K because it can degrade Keratin. The crystallization and molecular structure of Proteinase K indicates it belongs to subtilisin family, whose active site has a characteristic catalytic triple amino acid Asp39-His69-Ser224. Proteinase K has no significant substrate specificity and main cleavage site is the peptide bond at the carboxyl end of the hydrophobic amino acid such as aliphatic or aromatic. Recombinant Proteinase K is derived from yeast based on the optimized gene of Engyodontium album by site-directed mutation. It is purified by chromatography process and with calcium and glycerin as protective agents.