[en] Prebiotic isomaltooligosaccharide preparations contain α-D-glucooligosaccharides and their structure is the key factor for their prebiotic potential. The transglucosylation selectivity is known to depend on the enzyme specificity and moreover, maltose and -glucooligosaccharides can actually act as both glucosyl donor and acceptor in the reaction. Thus, two commercial enzymes, a glycosyl-tranferase and an -glucosidase, were tested alone and in combination on pure maltose to study their specificities and the IMO profile obtained. The reactions were monitored using a step-forward AEC-PAD analytical method which permitted to detect and resolve new unknown IMO. Structural determination of unknown IMO was attempt using their retention times and relative abundance. As a general rule, the -glucosidase has a more expressed hydrolyzing activity leading to products containing less residual digestible -(1-4) linkages such as isomaltose, isomaltotriose, isomaltotetraose, kojibiose and nigerose while the glucosyl-transferase produces important amount of panose. Finally, the combination of the two enzymes leaded to an intermediate IMO profile. IMO syrups composition was thus proved to be dependant on the specificity of the transglucosylating enzyme so that products profiles can be designed using different enzymes and in different proportion.
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