|Title||Enzymatic fingerprinting of isomalto/malto-polysaccharides|
|Author(s)||Zaal, P.H. van der; Klostermann, C.E.; Schols, H.A.; Bitter, J.H.; Buwalda, P.L.|
|Source||Carbohydrate Polymers 205 (2019). - ISSN 0144-8617 - p. 279 - 286.|
Biobased Chemistry and Technology
|Publication type||Refereed Article in a scientific journal|
|Keyword(s)||4,6-α-glucanotransferase - Glucanohydrolase - Starch - Substructure analysis - α-glucan|
In this study, we present an enzymatic fingerprinting method for the characterization of isomalto/malto-polysaccharides (IMMPs). IMMPs are produced by the modification of starch with the 4,6-α-glucanotransferase (GTFB) enzyme and consist of α-(1→4), α-(1→6) and α-(1→4,6) linked glucoses. Enzymes were used separately, simultaneously or in successive order to specifically degrade and/or reveal IMMP substructures. The enzymatic digests were subsequently analysed with HPSEC and HPAEC to reveal the chain length distribution (CLD) of different IMMP substructures. The presence of amylose in the substrate resulted in the formation of linear α-(1→6) linked glycosidic chains (13.5 kDa) in the former amylopectin fraction. The length of these chains indicates that GTFB transferase activity on amylopectin is more likely to elongate single amylopectin chains than to provide an even distribution. Enzymatic fingerprinting also revealed that the GTFB enzyme is capable of introducing large (20 kDa) linear α-(1→6) linked glycosidic chains in the α-glucan substrate.