Streptomyces rimosus extracellular proteases |
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Authors: | M. Renko Lj. Vitale M. Kokalj M. Pokorny |
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Affiliation: | (1) Joef Stefan Institute, 61000 Ljubljana, Yugoslavia;(2) Ruder Bokovi Institute, Bijenika c. 54, 41001 Zagreb, Yugoslavia;(3) Krka Pharmaceutical and Chemical Works, Research and Development Institute, 68000 Novo mesto, Yugoslavia |
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Abstract: | Summary A trypsin-like proteinase was isolated from Streptomyces rimosus culture filtrates obtained from an oxytetracycline production process. The isolation procedure includes ultrafiltration, chromatography on CM-Sephadex, AH-Sepharose and CM-cellulose and gives a homogeneous protein with 19% yield. The enzyme is an anionic trypsin (Mr 28 000, pI 4.5), is stable from pH 4.5 to 9 and up to 40°C, and contains three disulphide bridges, three histidines and three methionines per molecule. At its pH optimum (pH 8.4–8.8) it splits peptide, ester and arylamide bonds of arginine in the endo-position and, to a smaller extent, in the exo-position. Like other streptomycete trypsins, it is a more efficient catalyst than bovine trypsin and has a relative preference for peptide-arylamides, N-benzyloxycarbonyl-l-norleucyl-l-prolyl-l-arginine-p-nitroanilide being by far its best substrate. |
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