Purification and Some Properties of Glucodextranase from ArthrobacteY globiformis T-3044

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Glucodextranase was purified to homogeneity by means of affinity column chromatography, hydro-phobic, anion exchange and molecular-sieve HPLC from the culture of Arthrobacter globiformis T-3044 isolated from soil. The Mr of the enzyme was estimated to be 120 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The enzyme had an optimum pH for activity at pH 6.0, and was stable at pH 6.0 to 7.5 at 25°C for 24h. It was stable up to 40°C and was almost completely inactivated at 50deg;C for 15 min. The enzyme produced only β-D-glucose from dextran. The enzyme also hydrolyzed starch at about 15% of the hydrolysis ratio to dextran. This ratio was about 15 times higher than that of I42 GDase. The enzyme is characterized by a high activity toward starch.
日本応用糖質科学会の論文