Publications Scientifiques

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    Characterization of a purified thermostable xylanase from caldicoprobacter algeriensis sp. nov. strain TH7C1T
    (Elsevier, 2016) Bouanane-Darenfed, Amel; Boucherba, Nawel; Bouacem, Khelifa; Gagaoua, Mohammed; Joseph, Manon; Kebbouche-Gana, Salima; Nateche, Farida; Hacene, Hocine; Ollivier, Bernard; Cayol, Jean-Luc; Fardeau, Marie-Laure
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    Purification and characterization of a milk-clotting protease from Mucor pusillus : method comparison
    (Academic Journals, 2011) Nouani, A.; Moulti-Mati, F.; Belbraouet, S.; Bellal, M.M.
    Crude enzymatic extract obtained from five fermentations (300 g of wheat bran) was characterized by a clotting activity of 0.34 ± 0.08 UP/ml with a strength ratio of 1/1: 200. The comparative study of the summaries from 2 purification protocols showed that it is possible to recover 6% of the initial proteins with a 44.54% activity after gel filtration (protocol I), which appeared more technically sound when compared to ion-exchange (1.80% of total proteins with a 23% performance) (protocol II). The protein homogeneity (a single electrophoretic band) of the monomeric protease was confirmed by both methods after precipitation with 80% saturated ammonium sulphate. Moreover, the fractional precipitation technique with this salt (40 and 80%) was useless in the experimental conditions employed and an important loss of activity was observed (28.53%) with a 3-fold purification. In another part of the study, without ammonium sulphate precipitation, the gel filtration enabled the elimination of almost 97% of the inactive proteins and improved the activity performance by 55.13%, while multiplying the specific activity of the coagulant by a factor of 20.88 against a 6.75-fold purification with ionexchange and the appearance of a more or less 20 kDa peptide after electrophoresis. The proteolytic activity of the purified extracts had a similar appearance to a more pronounced kinetic when compared with the reference rennet. The purification protocols did not seem to have an impact on the isolated protease activity
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    Extracellular protease from mucor pusillus : purfication and characterization
    (2009) Nouani, A.; Belhamiche, N.; Slimani, R.; Fazouane, F.; Belbraouet, S.; Bellal, M.
    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