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Serine alkaline proteases from Cephalosporium sp. KM388 were specific against esters of aromatic and hydrophobic amino acids. Against oxidized insulin B-chain, the enzymes initially cleaved the site of Leu-Tyr(15-16). The cleavage specificity of KM388 protease D was broader than those of other alkaline proteases, and the site of Arg-Gly(22-23) was cleaved, which is a specific site for trypsin-like protease.

Substrate Specificity of Alkaline Proteases fromCephalosporiumsp. KM388