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
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.