Abstract
1. A barley glucan with 68% of β-(1→4)-linkages and 32% of β-(1→3)-linkages was exhaustively hydrolysed with an Aspergillus niger β-(1→4)-glucan 4-glucanohydrolase (EC 3.2.1.4) (Clarke & Stone, 1965b). The hydrolysis products were separated and estimated. 2. The lower-molecular-weight products were identified as: glucose, 1·4%; cellobiose, 11·9%; 32-O-β-glucosylcellobiose, 45·0%; a tetrasaccharide(s), which was a substituted cellobiose, 16·4%. A series of unidentified higher-molecular-weight products (26·5%) were also found. 3. The identity of the products suggests that the A. niger β-(1→4)-glucan hydrolase hydrolyses β-glucosidic linkages joining 4-O-substituted glucose residues. 4. When an enzyme fraction containing the β-(1→4)-glucan hydrolase and an exo-β-(1→3)-glucan hydrolase was used, the same products were found, but the higher-molecular-weight products were observed to have only a transient existence in the hydrolysate and were virtually absent after prolonged incubation. It is suggested that these oligosaccharides are resistant to attack by β-(1→4)-glucan hydrolase but are partially hydrolysed by the exo-β-(1→3)-glucan hydrolase and therefore possess one or more (1→3)-linked glucose residues at their non-reducing end.
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Selected References
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