Sequential starch modification by branching enzyme and 4-α-glucanotransferase improves retention of curcumin in starch-alginate beads

Carbohydr Polym. 2024 Jan 1:323:121387. doi: 10.1016/j.carbpol.2023.121387. Epub 2023 Sep 13.

Abstract

A new super-branched amylopectin with longer exterior chains was produced from normal maize starch by modification with branching enzyme followed by 4-α-glucanotransferase, and applied for co-entrapment of a curcumin-loaded emulsion in alginate beads. The network structure of the gel beads was obtained with Ca2+-cross-linked alginate and a modest load of retrograded starch. The dual enzyme modified starch contained more and longer α-1,6-linked branch chains than single enzyme modified and unmodified starches and showed superior resistance to digestive enzymes. Alginate beads with or without starch were of similar size (1.69-1.74 mm), but curcumin retention was improved 1.4-2.8-fold in the presence of different starches. Thus, subjecting the curcumin-loaded beads to in vitro simulated gastrointestinal digestion resulted in retention of 70, 43 and 22 % of the curcumin entrapped in the presence of modified, unmodified, or no starch, respectively. Molecular docking provided support for curcumin interacting with starch via hydrogen bonding, hydrophobic contacts and π-π stacking. The study highlights the potential of utilizing low concentration of dual-enzyme modified starch with alginate to create a versatile vehicle for controlled release and targeted delivery of bioactive compounds.

Keywords: Curcumin emulsion; Enzymatic modification; In vitro digestion; Release models; Starch-alginate beads.

MeSH terms

  • 1,4-alpha-Glucan Branching Enzyme*
  • Alginates / chemistry
  • Curcumin* / chemistry
  • Molecular Docking Simulation
  • Starch / chemistry

Substances

  • Starch
  • 1,4-alpha-Glucan Branching Enzyme
  • Curcumin
  • 4 alpha-glucanotransferase
  • Alginates