Extracellular protease from Mucor pusillus: purification and characterization |
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| Authors: | A NOUANI N BELHAMICHE R SLAMANI S BELBRAOUET F FAZOUANE M M BELLAL |
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| Affiliation: | Department of Food Technology, University of Boumerdès, Boumerdès, Algeria,;National Agronomic Institute, Algiers, Algeria,;Food Sciences Laboratory, National Institute of Agronomic Research, Algeria,;Ecole de Nutrition, Universitéde Moncton, Moncton, Canada |
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| Abstract: | Extracellular protease from Mucor pusillus was purified 18-fold with 7.56% recovery by ion-exchange chromatography and gel filtration. The enzyme was found to be monomeric in nature, having a molecular mass of 49 kDa. The enzyme acted optimally at 50°C and was stable in the temperature range 30–50°C. It was completely inactivated by heating for 30 min at 65°C. The optimum of activity for the purified extract was observed at milk CaCl2 concentration of 0.02 m and at milk pH of 5. These properties, except for temperature, were similar to those of rennet. |
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| Keywords: | Rennet Mucor pusillus Milk-clotting activity Purification |
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