An Isomaltotriose-producing Dextranase fromFlavobacteriumsp. M-73: Purification and Properties

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Abstract
An isomaltotriose-producing dextranase II, detected in the culture supernatant of Flavobacterium sp. M-73, was purified to an electrophoretically pure state. Successive chromatography on hydrophobic columns of Amberlite CG-50 and aminooctyl-Sepharose was very effective as the first step of purification. Further purification of the enzyme was performed by affinity column chromatography on isomaltotriose-Sepharose and preparative polyacrylamide gel electrophoresis. The purified enzyme was shown to be a monomer and had a molecular weight of 114,000. Dextranase II was most active at pH 7.0 and 35°C. It was stable at 4°C for 24 hr over a pH range of 6.5∼12.0 and up to 35°C on heating for 10 min. This enzyme had a strict specificity for consecutive α-l,6-glucosidic linkages and readily hydrolyzed clinical dextran and Sephadex gels. The degree of hydrolysis of clinical dextran was 31% expressed as apparent conversion into D-glucose. The amount of isomaltotriose in the hydrolyzate was determined to be 63%.

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