CYCLODEXTRINS ARE NOT THE MAJOR CYCLIC ALPHA-1,4-GLUCANS PRODUCED BY THE INITIAL ACTION OF CYCLODEXTRIN GLUCANOTRANSFERASE ON AMYLOSE

Citation
Y. Terada et al., CYCLODEXTRINS ARE NOT THE MAJOR CYCLIC ALPHA-1,4-GLUCANS PRODUCED BY THE INITIAL ACTION OF CYCLODEXTRIN GLUCANOTRANSFERASE ON AMYLOSE, The Journal of biological chemistry, 272(25), 1997, pp. 15729-15733
Citations number
27
Categorie Soggetti
Biology
ISSN journal
00219258
Volume
272
Issue
25
Year of publication
1997
Pages
15729 - 15733
Database
ISI
SICI code
0021-9258(1997)272:25<15729:CANTMC>2.0.ZU;2-3
Abstract
The initial acl;ion of cyclodextrin glucanotransferase (CGTase, EC 2.4 .1.19) from an alkalophilic Bacillus sp. A2-5a on amylose was investig ated. Synthetic amylose was incubated with purified CGTase then termin ated in the very early stage of the enzyme reaction. When the reaction mixture was treated with glucoamylase and the resulting glucoamylase- resistant glucans were analyzed with high performance anion exchange c hromatography, cyclic alpha-1,4-glucans, with degree of polymerization ranging from 9 to more than 60, in addition to well known alpha-, bet a-, and gamma-cyclodextrin (CD), were detected. The time-course analys is revealed that larger cyclic alpha-1,4-glucans were preferentially p roduced in the initial stage of the cyclization reaction and were subs equently converted into smaller cyclic alpha-1,4-glucans and into the final major product, beta-CD. CGTase from Bacillus macerans also produ ced large cyclic alpha-1,4-glucans except that the final major product was alpha-CD. Based on these re suits, a new model for the action of CGTase on amylose was proposed, which may contradict the widely held v iew of the cyclization reaction of CGTase.