Deciphering molecular interaction and digestibility in retrogradation of amylopectin gel networks.

The impact of the internal part of aewx amylopectin on the gel network and digestibility during retrogradation was investigated using wx amylopectin as a reference. After β-amylolysis for 60 min (aewx-60), greater shifts in both λmax value and absorbance of iodine binding profiles were observed, accompanied by an increment of short chains (DP 3-5) with reducing the external long chains (DP 17.2). For the amylopectin gels aged 7 days at 4 °C, aewx had greater intermolecular aggregation of double helices to form junction zones, resulting in remarkably higher G', which was significantly greater than that of wx amylopectin or aewx-60. Moreover, aewx amylopectin had a greater RS accompanied by a reduction in RDS after retrogradation. The gel network models of retrograded amylopectins were built to interpret more molecular interactions for aewx than those of wx. The results revealed that aewx amylopectin with a higher proportion of longer external chains prompted the flexibility to align and interact for the formation of double helices and enzyme-resistant structures.