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, Nα-benzyloxycarbonyl-l-norleucyl-l-prolyl-l-arginine-p-nitroanilide being by far its best substrate.
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Renko, M., Vitale, L., Kokalj, M. et al. Streptomyces rimosus extracellular proteases. Appl Microbiol Biotechnol 31, 38–44 (1989). https://doi.org/10.1007/BF00252523
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DOI: https://doi.org/10.1007/BF00252523