Effect of linear charge density of polysaccharides on interactions with α-amylase: Self-Assembling behavior and application in enzyme immobilization

The co-existence of polysaccharides and enzymes in the food matrix could form complexes that directly influence the catalytic efficacy of enzymes. This work investigated the self-assembly behaviors of α-amylase and charged polysaccharides and fabricated the α-amylase/polysaccharides complex coacervates. The results showed that the linear charge density of polysaccharides had a critical impact on the complex formation, structure, and enzyme protection under acidic conditions. At low pH, α-amylase formed compact and tight coacervates with the λ-carrageenan. However, α-amylase/pectin coacervates dissociated when the pH was lower than 3.0. The optimized binding ratio of α-amylase/λ-carrageenan was 12:1, and α-amylase/pectin was 4:1. Finally, the α-amylase/λ-carrageenan complex coacervates effectively immobilized the enzyme and almost 70% of enzyme activity remained in coacervates after exposure to pH3.0 for 1 h. This study demonstrates that the change in the linear charge density of polysaccharides could regulate the enzyme-catalyzed process in food processing by a simple and fine-controlled method.