Endo-1,4-L-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 50^55³C. It was stable for 48 h between pH 4.5 and 9.0, and for 1 h up to 60³C. The enzyme activity was strongly inhibited by Hg P , Ag P , Cu P , Mn P , and Cr P . The amino acid composition of the enzyme was in the order Asx s Glx s Leu s Try s Ser. ß 1998 Federation of European Microbiological Societies. Published by Elsevier Science B.V.
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