Some Catalytic Properties of an Exo-l,6-α-glucosidase (Glucodextranase) fromArthrobacter globiformisI42

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Abstract
An exo-l,6-α-glucosidase (EC 3.2.1.70) (glucodextranase) produced extraceUularly by Arthrobacter globiformis I42 was found to invert the configuration of glucose released from dextran, and to require calcium for protection against warming. Among isomaltodextrins used as substrates for this enzyme, the rate of hydrolysis for isomaltose was the lowest and increased with the degree of polymerization (d. p.) of the saccharides up to d. p. 7. The minor activities accompanying purified glucodextranase preparations (release of glucose from starch, splitting of maltose, nigerose and kojibiose) were ascribed to the glucodextranase itself. Fourteen native dextrans and soluble potato starch were subjected to digestion by this glucodextranase and the rate, process and extent of hydrolysis of these substrates were studied relative to the composition of non-l,6-α-linkages of these polysaccharides.