Abstract
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).
Highlights
Cellulose is one of the most abundant organically produced compounds available in the world and is a kind of sustainable energy which human beings are able to utilize (Bataillon et al, 2000)
For increasing the efficiency of the process, we could search of a more active cellulase or developing low-cost methods of pretreatment for the substrates, by making more accessible them suitable for enzymatic degradation. To mitigate of this problem, the purpose of the present study has been purified and characterized an endoglucanase producing by Streptomyces sp. strain BPNG23
The results show that the purified endoglucanase has more affinity for carboxymethyl cellulose (CMC) with a relative activity of 100%
Summary
Cellulose is one of the most abundant organically produced compounds available in the world and is a kind of sustainable energy which human beings are able to utilize (Bataillon et al, 2000). A complete degradation of cellulose implies a complex interaction with different cellulolytic enzymes It was widely agreed and accepted for three types of cellulolytic enzymes which include endoglucanases (EC 3.2.1.4) hydrolyze randomly internal glycosidic linkages in cellulose, whereas exoglucanases cleave long chains of the ends in the progressive chain, β-glucosidases transform cellobiose into glucose (Beg, 2001). The degradation of cellulose, hemicelluloses and lignin, that are abundant of plants, various strains from the Streptomyces genus were studied, and were found as good cellulase producers (Budihal and Patil, 2016; Shaik et al, 2017; Wu et al, 2017; Gobalakrishnan and Sivakumar, 2017; Schrempf, 2017; Kumarand Henehan, 2017). To mitigate of this problem, the purpose of the present study has been purified and characterized an endoglucanase producing by Streptomyces sp. strain BPNG23
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