Effect of linear charge density of polysaccharides on interactions with α-amylase: Self-Assembling behavior and application in enzyme immobilization
Effect of linear charge density of polysaccharides on interactions with α-amylase: Self-Assembling behavior and application in enzyme immobilization
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多糖线性电荷密度对与α-淀粉酶相互作用的影响：自组装行为及其在酶固定化中的应用
DOI：
10.1016/j.foodchem.2020.127320
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发表时间：
2020-11-30
期刊：
影响因子：
8.8
通讯作者：
Huang, Qingrong
中科院分区：
文献类型：
--
作者：
Jin, Weiping;Wang, Zhifeng;Huang, Qingrong
多糖和酶在食品基质中共存可形成复合物，直接影响酶的催化功效。这项工作研究了α-淀粉酶和带电多糖的自组装行为，并制备了α-淀粉酶/多糖复合凝聚层。结果表明，多糖的线性电荷密度对酸性条件下复合物的形成、结构和酶保护具有关键影响。在低 pH 值下，α-淀粉酶与 lambda-卡拉胶形成紧密且紧密的凝聚层。然而，当 pH 值低于 3.0 时，α-淀粉酶/果胶凝聚体会解离。 α-淀粉酶/λ-卡拉胶的优化结合比为12:1，α-淀粉酶/果胶为4:1。最后，α-淀粉酶/λ-卡拉胶复合物凝聚层有效地固定了酶，并且在暴露于pH3.0 1小时后几乎70%的酶活性保留在凝聚层中。这项研究表明，多糖线性电荷密度的变化可以通过简单且精细控制的方法来调节食品加工中的酶催化过程。
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 alpha-amylase and charged polysaccharides and fabricated the alpha-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, alpha-amylase formed compact and tight coacervates with the lambda-carrageenan. However, alpha-amylase/pectin coacervates dissociated when the pH was lower than 3.0. The optimized binding ratio of alpha-amylase/lambda-carrageenan was 12:1, and alpha-amylase/pectin was 4:1. Finally, the alpha-amylase/lambda-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.