Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 545509
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.
DOI https://doi.org/10.1016/j.carbpol.2018.09.049
Department(s) Biobased Chemistry and Technology
Food Chemistry
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2019
Keyword(s) 4,6-α-glucanotransferase - Glucanohydrolase - Starch - Substructure analysis - α-glucan
Abstract

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.

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