Effects of pullulanase debranching on the properties of potato starch-lauric acid complex and potato starch-based film.
Amylose-lipid complex
Debranching time
Potato starch
Potato starch-based films
Journal
International journal of biological macromolecules
ISSN: 1879-0003
Titre abrégé: Int J Biol Macromol
Pays: Netherlands
ID NLM: 7909578
Informations de publication
Date de publication:
01 Aug 2020
01 Aug 2020
Historique:
received:
22
05
2019
revised:
25
08
2019
accepted:
20
11
2019
pubmed:
25
11
2019
medline:
11
3
2021
entrez:
25
11
2019
Statut:
ppublish
Résumé
The effects of different debranching time on the properties of potato starch and its films were evaluated. Potato starch granules were debranched with pullulanase for 0, 0.5, 1.0, 1.5 or 2.0 h. The effects of pullulanase debranching treatment on the chain-length distributions of amylopectin were analysed by high performance anion exchange chromatography (HPAEC), which proved that the shorter debranching treatment generated more linear chains with favourable lengths to facilitate the formation of potato starch-lauric acid complexes. The debranched starch-lipid complexes showed higher lauric acid content than that of the untreated sample. X-ray diffraction showed that the diffraction intensity of the debranched sample was stronger than that of the undebranched sample, and when the debranching time was >1.5 h, the diffraction intensity and relative crystallinity of the complexes decreased. The sample exhibited a high melting enthalpy (ΔH) under the pullulanase debranching treatment for 1.5 h. Scanning electron microscope data indicated that the surface of the composite film was flatter after the debranching treatment and that the films exhibited the lowest water vapour permeability and highest tensile strength after the treatment time for 1.5 h.
Identifiants
pubmed: 31760002
pii: S0141-8130(19)33801-2
doi: 10.1016/j.ijbiomac.2019.11.173
pii:
doi:
Substances chimiques
Lauric Acids
0
lauric acid
1160N9NU9U
Starch
9005-25-8
Glycoside Hydrolases
EC 3.2.1.-
pullulanase
EC 3.2.1.41
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
1330-1336Informations de copyright
Copyright © 2019 Elsevier B.V. All rights reserved.