Streptomyces rimosus extracellular proteases
| Autor: | M. Pokorny, M. Kokalj, M. Renko, Lj. Vitale |
|---|---|
| Rok vydání: | 1989 |
| Předmět: |
chemistry.chemical_classification
biology Stereochemistry Streptomycetaceae Streptomyces rimosus Substrate (chemistry) Peptide General Medicine biology.organism_classification Trypsin Applied Microbiology and Biotechnology Ultrafiltration (renal) Enzyme chemistry medicine Actinomycetales Biotechnology medicine.drug |
| Zdroj: | Applied Microbiology and Biotechnology. 31 |
| ISSN: | 1432-0614 0175-7598 |
| DOI: | 10.1007/bf00252523 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full text from SpringerLink