The mechanism of carbohydrase action. 10. Enzymic synthesis and properties of 6-α-maltosylglucose
- 1 March 1964
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 90 (3) , 616-620
- https://doi.org/10.1042/bj0900616
Abstract
The coupling reaction between cyclomalto-hexaose and isomaltose, catalysed by Bacillus macerans transglycosylase, was carried out and the products were degraded with [beta]-amylase. A tri-saccharide, proved to be 6-[alpha]-maltosylglucose, was isolated as a [beta]-amylase-resistant end product. A tetrasaccharide, believed to be 6-[alpha]-maltotriosylglucose, was also isolated. This was slowly hydrolysed by [beta]-amylase. The rate of hydrolysis of 6-[alpha]-maltosylglu-cose in hot aqueous acid is the same as of the isomeric trisaccharide panose (4-[alpha]-isomaltosylglucose).This publication has 9 references indexed in Scilit:
- The mechanism of carbohydrase action. 9. Hydrolysis of salep mannan by preparations of α-amylaseBiochemical Journal, 1963
- Polysaccharides Elaborated by Pullularia pullulans. Part II. The Partial Acid Hydrolysis of the Neutral Glucan Synthesised from Sucrose Solutions.Acta Chemica Scandinavica, 1963
- The mechanism of carbohydrase action. 8. Structures of the muscle-phosphorylase limit dextrins of glycogen and amylopectinBiochemical Journal, 1960
- Preparation and characterization of the isomaltodextrinsBiochemical Journal, 1957
- ACTION OF BETA-AMYLASE ON BRANCHED OLIGOSACCHARIDES1956
- Use of Ion-Exchange Resins in Paper Chromatography of SugarsNature, 1953
- Detection of Sugars on Paper ChromatogramsNature, 1950
- Preparation and Properties of the Amylases Produced by Bacillus macerans and Bacillus polymyxaJournal of Bacteriology, 1942