The 92-kDa chitinase from Streptomyces olivaceoviridis contains a lysine-C endoproteinase at its N-terminus |
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Authors: | HH Radwan HJ Plattner U Menge H Diekmann |
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Institution: | Institut für Mikrobiologie, Universität Hannover, Schneiderberg 50, 30167 Hannover, FRG; Gesellschaft für Biotechnologische Forschung, Mascheroder Weg 1, 38124 Braunschweig, FRG |
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Abstract: | Abstract Serine proteinases of 42, 22 and 14 kDa were purified from the culture fluid of Streptomyces olivaceoviridis by FPLC. The first 14 amino acids at their N-termini were identical and coincide with the N-terminal amino acid sequence of 92-kDa chitinase, which was found to hydrolyse casein. The four proteins hydrolyse synthetic substrates at the carboxyl group of lysine and (more slowly) arginine. The 14-kDa endoproteinase releases only two fragments of 42 and 43 kDa from β-galactosidase. When the pure 92-kDa chitinase was incubated at 37°C in Tris·HCl buffer, it was cleaved into a 70-kDa chitinase and a 22-kDa proteinase which in its part is rapidly degraded to a 14-kDa proteinase. |
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Keywords: | Streptomyces olivaceoviridis Chitinase Serine proteinase Autocatalytic degradation |
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