Activated effect of lignin on α-amylase.
Activated effect of lignin on α-amylase.
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DOI：
10.1016/j.foodchem.2013.05.047
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发表时间：
2013-12
期刊：
影响因子：
8.8
通讯作者：
Juan Zhang;Junhui Cui;Tingting Yin;Lizhou Sun;Genxi Li
中科院分区：
文献类型：
--
作者：
Juan Zhang;Junhui Cui;Tingting Yin;Lizhou Sun;Genxi Li
本文报道了一种新的α-淀粉酶激活剂--木质素，它能显著提高α-淀粉酶的活力。木质素对α-淀粉酶的促进作用比传统的α-淀粉酶激活剂氯离子更强。进一步的实验结果表明，木质素可以与α-淀粉酶相互作用，形成1：1的复合物，结合常数为4.47 × 105M − 1。结合是自发的，木质素/α-淀粉酶复合物的形成是一个外显反应。在结合过程中，氢键起着关键作用，非辐射能量从α-淀粉酶转移到木质素。木质素与α-淀粉酶的结合符合一级指数衰减函数。木质素/α-淀粉酶复合物的形成导致α-螺旋含量从57.7%降低到53.9%，色氨酸残基周围极性增加，疏水性降低，蛋白颗粒体积增大。这项工作将使人们更深入地了解木质素作为一种膳食纤维，被称为一种重要的食品功能因子。此外，它还有助于开发用于食品工业的α-淀粉酶激活剂。
This paper reports a new kind of activator of α-amylase, lignin, which can greatly increase α-amylase activity. The promoted ratio of lignin is even much higher than that of chloride ion, the traditional activator of α-amylase. Further experimental results reveal that lignin may interact with α-amylase to form a 1:1 complex with a binding constant of 4.47 × 105M−1. The binding is spontaneous and lignin/α-amylase complex formation is an exothermal reaction. Hydrogen bonding plays a key role and non-radiation energy transfers from α-amylase to lignin in the binding process. Lignin, combining with α-amylase, conforms to a first-order exponential decay function. The formation of the lignin/α-amylase complex results in the reduction of α-helical content from 57.7% to 53.9%, the increase of the polarity around tryptophan residues, the decrease of the hydrophobicity, and the enlargement of protein granule volume. This work will give a deeper insight into lignin as a kind of dietary fibre, known as an important food functional factor. Furthermore, it also contributes to the exploration of an activator of α-amylase, used in the food industry.