Purification and characterization of an extracellular proline iminopeptidase from Corynebacterium variabilis NCDO 2101
| Autor: | Patrick F. Fox, E. Smacchi, Rosalba Lanciotti, T. Cogan, M. Semeraro, Marco Gobbetti |
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| Rok vydání: | 2001 |
| Předmět: |
Proteolysis
Corynebacterium variabilis Cheese ripening Biology Corynebacterium Sodium Chloride Applied Microbiology and Biotechnology Aminopeptidases chemistry.chemical_compound Cheese medicine Extracellular chemistry.chemical_classification medicine.diagnostic_test Temperature food and beverages Ripening General Medicine Hydrogen-Ion Concentration biology.organism_classification Lactic acid Enzyme Biochemistry chemistry Bacteria Biotechnology |
| Zdroj: | Journal of applied microbiology. 90(3) |
| ISSN: | 1364-5072 |
| Popis: | Aims: To screen the extracellular proteolytic and lipolytic activities of Corynebacterium variabilis NCDO 2101 and to purify and characterize a proline iminopeptidase enzyme in order to investigate the role of the major component of the smear of bacterial surface-ripened cheeses. Methods and Results: Four chromatographic steps were used to purify the enzyme and a three-factor, five-level Central Composite Design was used to study the interactive effects of cheese-related values of pH, NaCl and temperature. The proline iminopeptidase showed some biochemical properties different from the same enzyme purified from lactic acid bacteria and other smear bacteria. It tolerated NaCl concentrations up to 7·5% and was sensitive to low values of pH especially when they were combined with low temperature. Conclusions: The proline iminopeptidase of C. variabilis NCDO 2101 may have a role in proteolysis during ripening of smear surface-ripened cheeses. Significance and Impact of the Study: The findings of this work contribute to the knowledge of the enzymology of smear bacteria in order to improve the ripening of bacterial surface-ripened cheeses. |
| Databáze: | OpenAIRE |
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