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

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.