Enzymatic fingerprinting of isomalto/malto-polysaccharides.
4,6-α-glucanotransferase
Glucanohydrolase
Starch
Substructure analysis
α-glucan
Journal
Carbohydrate polymers
ISSN: 1879-1344
Titre abrégé: Carbohydr Polym
Pays: England
ID NLM: 8307156
Informations de publication
Date de publication:
01 Feb 2019
01 Feb 2019
Historique:
received:
18
05
2018
revised:
15
09
2018
accepted:
18
09
2018
entrez:
18
11
2018
pubmed:
18
11
2018
medline:
20
12
2018
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 30446106
pii: S0144-8617(18)31123-8
doi: 10.1016/j.carbpol.2018.09.049
pii:
doi:
Substances chimiques
Amylose
9005-82-7
Amylopectin
9037-22-3
Amylases
EC 3.2.1.-
Glycoside Hydrolases
EC 3.2.1.-
isopullulanase
EC 3.2.1.57
Isoamylase
EC 3.2.1.68
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
279-286Informations de copyright
Copyright © 2018 Elsevier Ltd. All rights reserved.