Evidence for α-1,6 and α-1,4-glucosidic bond cleavage in highly branched glycogen by amylopullulanase fromThermoanaerobacter ethanolicus
✍ Scribed by Saroj P. Mathupala; Jong-Hyun Park; J. Gregory Zeikus
- Book ID
- 104642968
- Publisher
- Springer Netherlands
- Year
- 1994
- Tongue
- English
- Weight
- 359 KB
- Volume
- 16
- Category
- Article
- ISSN
- 0141-5492
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✦ Synopsis
Activity of amylopullulanase from Thermoanaerobacter ethanolicus 39E on a-1,6 and a-1,6glucosidic linkages in highly branched mammalian glycogen was analyzed by paper chromatography and 13C nuclear magnetic resonance (NMR) spectroscopy. Paper chromatography analysis showed that the glycogen hydrolysate consisted of glucose, maltose, maltotriose and maltotetraose. NMR spectroscopy confirmed that no hydrolysate products of a-1,6 linkage were present resulting from treatment with the amylopullulanase. Therefore, the amylopullulanase efficiently hydrolyzed glycogen both at a-1,6-and at a-1,4-glucosidic linkages into oligosaccharides.