Effect of Debranching Enzymes on Self-Assembly Kinetics and Physicochemical Characteristics of Short-Chain Glucan Aggregates (SCGAs)

Characteristics of short-chain glucan aggregates (SCGAs) prepared with two different debranching enzymes, isoamylase (I-SCGA) and pullulanase (P-SCGA), were investigated. In terms of self-assembly and crystallization kinetics, I-SCGA exhibited a faster SCGA formation rate, while P-SCGA demonstrated a rapid crystallization rate. P-SCGA had a higher amount of glucan chains with DP ≤ 12, whereas I-SCGA showed a significantly higher amount of B1 chains (13 ≤ DP ≤ 24). Both SCGAs formed aggregates with average sizes of 990 nm (P-SCGA) and 810 nm (I-SCGA), respectively. P-SCGA displayed a wider double-helical melting transition temperature range and higher melting enthalpy than I-SCGA. Although both SCGAs revealed similar amounts of RDS content, P-SCGA showed significantly higher RS and lower SDS contents than I-SCGA. These results highlight the potential of using specific debranching enzymes to develop SCGA with targeted nutritional and functional properties, supporting the creation of customized starch ingredients for health-oriented food products.