Purification and Properties of Cyclomaltodyxtrinase from Alkalophilic Bacillus sp.

概要

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An alkalophilic strain isolated from soil produced intracellular cyclomaltodextrinase on the culture medium at an initial pH of 10.6. The strain was identified as closely resembling Bacillus circulans. The enzyme was purified 252-fold from the cell extract by chitosan treatment, ammonium sulfate fractionation, DEAE-Toyopearl column chromatography, and gel filtration. The pH and temperature optima of the purified enzyme were 6.0 and 50℃. THe molecular weight of the enzyme was 126,000,with two subunits of 67,000. The isoelectric point was pH 4.2. Enzyme activity was inhibited by Ag^+, Hg^<2+>, Cu^<2+>, and p-chloromercuribenzoate. The enzyme hydrolyzed α-, β-, and γ-cyclodextrins, as well as linear maltodextrins, to yield maltooligosaccharides. Starch and maltose were not degraded by the enzyme.
公益社団法人日本生物工学会の論文
1991-04-25