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Titre: Extracellular protease from mucor pusillus : purfication and characterization
Auteur(s): Nouani, A.
Belhamiche, N.
Slimani, R.
Fazouane, F.
Belbraouet, S.
Bellal, M.
Mots-clés: Rennet
Mucor pusillus
Milk-clotting activity
Purification
Date de publication: 2009
Collection/Numéro: International Journal of Dairy Technology/ Vol.62, N°1 (2009);pp. 112–117
Résumé: 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
URI/URL: http://dlibrary.univ-boumerdes.dz:8080/jspui/handle/123456789/357
Collection(s) :Publications Internationales

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