Purification and physicochemical properties of an extra-cellular cycloamylose (cyclodextrin) glucanotransferase from Bacillus macerans |
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Authors: | Arne Stavn Per Einar Granum |
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Institution: | Department of Microbiology, Norwegian Food Research Institute, P.O. Box 50, N-1432, Ås-NLH Norway |
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Abstract: | An extracellular cycloamylose (cyclodextrin) glucanotransferase (EC 2.4.1.19) from Bacillus macerans was purified to homogeneity by adsorption on starch, ammonium sulfate fractionation, column chromatography on DEAE-cellulose, and gel filtration on Sephadex G-100. The enzyme had a molecular weight of 67,000 and consisted of one polypeptide chain. The isoelectric point was pH 5.4. Temperature and pH optima were 60° and 5.45.8, respectively. The purified enzyme was quite stable at 50° (pH 6.0), but lost ≈80% of its activity at 60° for 30 min (pH 6.0). Prolonged digestion by trypsin did not affect the catalytic properties of the enzyme. The Km for starch was 5.7 mg/ml. |
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Keywords: | To whom correspondence should be addressed |
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