Structures of Singly Branched Heptaoses Produced by Bacterial Liquefying α-Amylase

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Abstract
1. A singly branched heptaose produced as a limit dextrin in the digest of β-limit dextrin with liquefying α-amylase [EC 3.2.1.1] of Bacillus amyloliquefaciens was isolated in a paper chromatographically pure state. 2. Analysis using several enzymes revealed that the isolated branched dextrin was a mixture of six singly branched heptaoses with different ramifying points. 3. All the branched heptaoses contained a 62-α-maltosylmaltotriose moiety in their molecules, differing only in the mode of attachment of one maltose or two glucose residues by α-1, 4-glucosidic bonds from this core dextrin. 4. The formation of various singly branched heptaoses (the present paper) and hexaoses (the previous paper) is discussed regarding the attack site specificity of the enzyme on β-limit dextrin.

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