Preparation and Enzymatic Hydrolysis of Maltosyl-α-cyclodextrin
- 1 December 1985
- journal article
- research article
- Published by Oxford University Press (OUP) in Agricultural and Biological Chemistry
- Vol. 49 (12) , 3391-3398
- https://doi.org/10.1080/00021369.1985.10867282
Abstract
Maltosyl-α-cyclodextrin (6-α-maltosylcyclomaltohexaose, M-CD) was prepared from maltose and α-cyclodextrin by the reverse action of Bacillus pullulanase, and the action of α-amylases on this dextrin was examined. Among α-amylases tested, Thermoactinomyces vulgaris α-amylase (TVA) and Taka-amylase A (TAA) were found to attack the M-CD. Their action pattern on M-CD was studied. These α-amylases cleaved, first the cyclodextrin ring of M-CD, and the branched octasaccharides formed were immediately degraded to form glucose, branched tetraose, or pentaose, though the action pattern was different for TVA and TAA. In addition, TAA also split M-CD into glucose and glucosyl-α-cyclodextrin. Fission products at various stages of the reaction were separated and analyzed by paper chromatography and high performance liquid chromatography, their structures were analyzed, and the degradation pattern of M-CD was found.Keywords
This publication has 8 references indexed in Scilit:
- Hydrolysis ofα-1,4- andα-l,6-Glucosidic Linkages in Trisaccharides by theThermoactinomyces vulgarisα-AmylaseAgricultural and Biological Chemistry, 1983
- Enzymatic Properties and Action Patterns ofThermoactinomyces vulgarisα-AmylaseAgricultural and Biological Chemistry, 1982
- A Pseudomonas intracellular amylase with high activity on maltodextrins and cyclodextrinsBiochimica et Biophysica Acta (BBA) - Enzymology, 1975
- Kinetic Studies on the Hydrolyses of α-, β-, and γ-Cyclodextrins by Taka-amylase A*1The Journal of Biochemistry, 1974
- Pullulan 4-glucanohydrolase from Aspergillus nigerArchives of Biochemistry and Biophysics, 1972
- PHYSICOCHEMICAL STUDIES ON TAKA-AMYLASE AThe Journal of Biochemistry, 1957
- Anomeric Inversions by GlycosidasesNature, 1955
- NOTES ON SUGAR DETERMINATIONJournal of Biological Chemistry, 1952