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Published on: October 29, 2013
Effect of linear charge density of polysaccharides on interactions with α-amylase: Self-Assembling behavior and
Weiping Jin1, Zhifeng Wang1, Dengfeng Peng2
1Hubei Key Laboratory for Processing and Transformation of Agricultural Products and College of Food Science and Engineering, Wuhan Polytechnic University, Wuhan 430023, China.
Abstract:
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.
