Key structural factors that determine the in vitro enzymatic digestibility of amylose-complexes.

The effects of complexing conditions on the formation of amylose-lipid-protein complexes and relationships between structure and digestion of amylose-lipid and amylose-lipid-protein complexes were poorly understood. The objective of this study was to investigate the effects of complexing time (0, 0.5, 2, 4 and 6 h) and temperature (60, 70, 80, 90 and 100 °C) on the structure and in vitro amylolysis of amylose-lauric acid (AM-LA) and amylose-lauric acid-β-lactoglobulin (AM-LA-βLG) complexes, and to understand the relationships between structure and in vitro digestiblity of these complexes. Longer complexing time and higher complexing temperature promoted the formation of greater amounts of the more stable type II crystallites than type I crystallites in both AM-LA and AM-LA-βLG complexes, which in turn decreased the rate and extent of the complexes digestion to a greater extent. Correlation analyses between parameters for structure and digestion kinetics showed that both the quantity of AM-LA and AM-LA-βLG complexes and the quality of their arrangement into V-type crystallites influenced their rate and extent of digestion. This study demonstrates that AM-LA and AM-LA-βLG complexes can be prepared with designed structural and functional properties tailored for various applications. [Display omitted] [ABSTRACT FROM AUTHOR]