1993 Volume 57 Issue 1 Pages 47-50
The detailed action mechanism of dextrin dextranase (EC 2.4.1.2, DDase) from Acetobacter capsulatus ATCC 11894 was investigated. DDase catalyzed the transglucosylation action of the non-reducing terminal glucosyl residue of a donor substrate, and three transglucosylation modes were recognized ; (1) transfer of an α-1, 4 linked glucosyl residue forming an α-1, 6 linkage, (2) transfer of an α-1, 4 linked glucosyl residue forming an α-1, 4 linkage, (3) transfer of an α-1, 6 linked glucosyl residue forming an α-1, 6 linkage. From these results, the action of DDase was considered to transfer α-1, 4 or α-1, 6 linked glucosyl residues at non-reducing termini of oligosaccharides to glucose molecules or glucosyl residues at non-reducing termini of other oligosaccharides forming α-1, 4 or α-1, 6 linkages. As the α-1, 6 linked terminal glucosyl residues were less reactive than α-1, 4 linked terminal glucosyl residues, DDase accumulated the α-1, 6 linked glucosyl residues, which is dextran.
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