Extracellular protease from mucor pusillus : purfication and characterization

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dc.contributor.authorNouani, A.
dc.contributor.authorBelhamiche, N.
dc.contributor.authorSlimani, R.
dc.contributor.authorFazouane, F.
dc.contributor.authorBelbraouet, S.
dc.contributor.authorBellal, M.
dc.date.accessioned2015-04-14T14:33:21Z
dc.date.available2015-04-14T14:33:21Z
dc.date.issued2009
dc.description.abstractExtracellular 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 renneten_US
dc.identifier.urihttps://dspace.univ-boumerdes.dz/jspui/handle/123456789/357
dc.language.isoenen_US
dc.relation.ispartofseriesInternational Journal of Dairy Technology/ Vol.62, N°1 (2009);pp. 112–117
dc.subjectRenneten_US
dc.subjectMucor pusillusen_US
dc.subjectMilk-clotting activityen_US
dc.subjectPurificationen_US
dc.titleExtracellular protease from mucor pusillus : purfication and characterizationen_US
dc.typeArticleen_US

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