Purification and characterization of an endo-1,4-β-mannanase from Bacillus subtilis KU-1

Endo-1,4-β-mannanase was purified to homogeneity from the culture supernatant of Bacillus subtilis KU-1 by ammonium sulfate precipitation, DEAE-Toyopearl, phenyl-Sepharose and FPLC Mono Q column chromatography by 810-fold with 39% yield. The molecular mass of the enzyme was estimated to be 39 kDa by SDS-PAGE and 40 kDa by gel filtration. It had a pI of 4.5 with maximum activity at pH 7.0 and 50–55°C. It was stable for 48 h between pH 4.5 and 9.0, and for 1 h up to 60°C. The enzyme activity was strongly inhibited by Hg2+, Ag2+, Cu2+, Mn2+, and Cr2+. The amino acid composition of the enzyme was in the order Asx>Glx>Leu>Try>Ser.

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