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Cyclic glucans produced by the intramolecular transglycosylation activity of potato D-enzyme on amylopectin
journal contribution
posted on 2023-05-18, 11:27 authored by Takaha, T, Yanase, M, Takata, H, Okada, S, Steven SmithSteven SmithPotato D-enzyme catalyses an intramolecular transglycosylation reaction on amylose to produce cycloamylose, a novel cyclic α-1,4 glucan. To determine if a similar activity could be observed with a high molecular weight branched substrate, recombinant potato D-enzyme was incubated with amylopectin. The substrate was converted into two fractions of lower molecular mass. Fraction I comprised 15% cyclic molecules of which the majority contained both α-1,4 and α-1,6 links. These were shown to be branched molecules with branches shorter than those in amylopectin. Fraction II comprised 80% cyclic molecules of which the majority contained only α-1,4 links (cycloamylose). Since fraction II appeared before fraction I, we propose that D-enzyme first catalysed the cyclisation of the outer side chains of amylopectin and then the cyclisation of inner chains to produce branched clusters. These results demonstrate that D-enzyme can catalyse the transfer of branched glucans, and suggest novel ways in which it may participate in starch metabolism in plants.
History
Publication title
Biochemical and Biophysical Research CommunicationsVolume
247Pagination
493-497ISSN
0006-291XDepartment/School
School of Natural SciencesPublisher
Academic Press Inc Elsevier SciencePlace of publication
525 B St, Ste 1900, San Diego, USA, Ca, 92101-4495Rights statement
Copyright 1998 Academic PressRepository Status
- Restricted