PURIFICATION AND CHARACTERIZATION OF AN ENDOGLUCANASE PRODUCED FROM Streptomyces sp. STRAINBPNG23

Streptomyces sp. strain BPNG23 produces five endoglucanases: endo1, endo 2, endo 3, endo 4 and endo 5.The endo2 has been purified and characterized by two subsequent purification steps with ultrafiltration and anion exchange chromatography. The specific activity of the endoglucanase has been found to be 380.65 U/mg. The molecular weight to the endoglucanase 2 has been estimated with sodium dodecyl sulfate-polyacrylamide gel electrophoresis, revealing that this isoenzyme is a 66 KDa monomeric enzyme. It showed an optimum temperature and pH values respectively of 6.0 and 50 °C. It was thermostable, it exhibited a half-life time 6 h with a temperature of 50 °C, the enzyme was activated by several metal ions Mn+2, NH4+, Zn2+, Ca2+, Fe2+, Ni2+ and Co2+. It presents a higher affinity towards carboxymethyl cellulose (CMC) with a Km of 6.37 mg/mL and Vmax of 0.056 μmol/mn. This the first of a study of purification and characterization of an endoglucanase produced by a newly isolated actinobacteria strain in Kabylia region (Algeria).