Enzymatic fingerprinting of isomalto/malto-polysaccharides
| Autor: | Johannes H. Bitter, Pieter Lykle Buwalda, P.H. van der Zaal, Henk A. Schols, C.E. Klostermann |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Glycoside Hydrolases
Polymers and Plastics Starch Biobased Chemistry and Technology Amylopectin 02 engineering and technology 010402 general chemistry Polysaccharide 01 natural sciences α-glucan chemistry.chemical_compound Amylose Levensmiddelenchemie Materials Chemistry Transferase 4 6-α-glucanotransferase 6-α-glucanotransferase Solanum tuberosum VLAG chemistry.chemical_classification Molecular Structure Food Chemistry Glucanohydrolase Organic Chemistry Substrate (chemistry) Glycosidic bond 021001 nanoscience & nanotechnology Substructure analysis 0104 chemical sciences Enzyme chemistry Biochemistry Amylases 0210 nano-technology Isoamylase |
| Zdroj: | Carbohydrate Polymers, 205, 279-286 Carbohydrate Polymers 205 (2019) |
| ISSN: | 0144-8617 |
| DOI: | 10.1016/j.carbpol.2018.09.049 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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