Purification and Characterization of a Milk Clotting Protease fromMucor bacilliformis
| Autor: | Elda R. Fraile, Mirtha Biscoglio de Jiménez Bonino, Liliana B. Areces, Osvaldo Cascone, Marina A. A. Parry, Héctor M. Fernández |
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| Rok vydání: | 1992 |
| Předmět: |
Proteases
medicine.medical_treatment Ion chromatography Bioengineering Applied Microbiology and Biotechnology Biochemistry chemistry.chemical_compound medicine Animals Aspartic Acid Endopeptidases Chymosin Amino Acids Molecular Biology Polyacrylamide gel electrophoresis Chromatography High Pressure Liquid chemistry.chemical_classification Chromatography Protease Chemistry Caseins General Medicine Hydrogen-Ion Concentration Chromatography Ion Exchange Culture Media Molecular Weight Kinetics Milk Enzyme Mucor Glycine Electrophoresis Polyacrylamide Gel Pepstatin Biotechnology |
| Zdroj: | Applied Biochemistry and Biotechnology. 37:283-294 |
| ISSN: | 1559-0291 0273-2289 |
| DOI: | 10.1007/bf02788880 |
| Popis: | An acid protease having milk clotting activity has been isolated from Mucor bacilliformis cultures. The enzyme was basically purified by ionic exchange chromatography. An average yield of 29 mg purified product was obtained from 100 mL crude extract. As purity criteria, SDS-PAGE, reverse-phase HPLC, and N-terminal analysis were performed. The protease is a protein composed of a single polypeptide chain with glycine at the N-terminus. The mol wt is approx 32,000, and its amino acid composition is very similar to those of other fungal proteases. As expected, its clotting activity was drastically inhibited by pepstatin A action. On the other hand, its instability against heat treatment and its clotting/proteolytic activity ratio indicate that it may be considered as a potential substitute for bovine chymosin. |
| Databáze: | OpenAIRE |
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