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KMID : 0380619810130010067
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Korean Journal of Food Science and Technology
1981 Volume.13 No. 1 p.67 ~ p.73
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Purification and Characterization of Streptomyces chibaensis Inulase
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Abstract
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An inulase from Streptomyces chibaensis was purified about 120-fold with the yield of 38 by ethanol precipitation, DEAE-cellulose chromatography and Sephadex G-200 gel-filtration. The purified enzyme showed the maximal activity at pH 6.5 and was fairly stable between pH 5.0∼9.0. The enzyme was slightly activated by Mn^(++), Mg^(++) and Co^(++), and :narkedly inactivated by Hg^(++) and Ag+. The inulase was characterized as a typical endo-inulase which hydrolyzed inulin in a random manner and Km for the inulin was 4.54×10^(-4)M.
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