Isolation, Purification and Characterization of Mannanase from Bacillus subtilis MAN-511
نویسندگان
چکیده
A bacterium, MAN-511 that produced extracellular mannanase, was isolated and identified as Bacillus subtilis on the basis of 16S rDNA phylogenetic analysis. The enzyme was purified to apparent homogeneity by precipitasi ammonium sulfat 70% and Sephadex G-75 chromatography procedures. The mannanase was purified 7.6 fold and specificity of 9.3 U/mg protein. SDS-PAGE of the purified enzyme showed a single protein band of molecular mass 45.08 kDa. The mannanase activity from this strain had optimum pH of 7.0, stable at a pH 6-7, optimum temperature at 30oC and stable at 30-40oC. In addition, crude mannanase preparation were successfully employed for the degradation of glucomanan which has been proved by reduce of viscosity.
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