Further characterization and kinetic parameter determination of a milk-clotting protease fromMucor bacilliformis |
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Authors: | Graciela D. Venera Claudia Machalinski Hugo Zum’arraga Mirtha J. Biscoglio Jim’enez de Bonino |
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Affiliation: | (1) Instituto de Qu’imica y Fisicoqu’imica Biol’ogicas (UBA-CONICET), Facultad de Farmac’a y Bioqu’im’ica Junin 956, 1113 Buenos Aires, Argentina |
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Abstract: | Further characterization of an aspartyl protease fromMucor bacilliformis with milk-clotting activity was performed. An extinction coefficient, ε278 cm = 1.61 mL/mg/cm, a molecular mass of 35,400 Da and a pI of 5.2 were determined. Proteolytic activity and kinetic parameters were evaluated by using the hexapeptide Leu-Ser-pNO2-Phe-Nle-Ala-Leu-OMe as the substrate. The effect of pH and temperature on peptide cleavage, as well as protease heat stability, was determined. Such properties, taken as a whole, indicate that theM. bacilliformis protease can be considered a potential substitute for bovine chymosin in cheese manufacture. |
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Keywords: | Mucor bacilliformis protease milk-clotting enzyme aspartyl protease fungal protease aspartyl protease kinetic parameters mesophilic enzyme cheese manufacture |
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