Inhibition of starch digestion: The role of hydrophobic domain of both α-amylase and substrates
Inhibition of starch digestion: The role of hydrophobic domain of both α-amylase and substrates
复制标题
淀粉消化的抑制：α-淀粉酶和底物的疏水域的作用
DOI：
10.1016/j.foodchem.2020.128211
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发表时间：
2021-03-30
期刊：
影响因子：
8.8
通讯作者：
Chen, Zhong-Xiu
中科院分区：
文献类型：
--
作者：
Liu, Qi-Zheng;Zhang, Hai;Chen, Zhong-Xiu
淀粉消化的理化机制非常复杂，淀粉酶抑制剂与底物或酶的非价相互作用可能影响淀粉消化。疏水相互作用在淀粉消化过程中的作用尚不清楚。本研究以不同疏水性的pluronics （PLs）为模型两亲化合物，采用多光谱方法研究其对淀粉消化的抑制作用。结果表明，PLs的疏水性改变了淀粉的结构，但对α -淀粉酶的结构影响更大，暴露了更多的色氨酸残基，增加了α -螺旋和β -片的含量。用不同链长的脂肪酸进一步研究证实了这一结果。本研究的发现为设计和制造α -淀粉酶抑制剂在分子水平上控制淀粉消化提供了信息。
The physicochemical mechanism of starch digestion is very complicated since it may be affected by the non-valence interactions of the amylase inhibitor with the substrate or the enzyme. The role of hydrophobic interaction in the process of starch digestion is not clear. In this study, pluronics (PLs) with different hydrophobicity were used as model amphiphilic compounds to study their inhibition on starch digestion using multi-spectroscopic methods. The results showed that the hydrophobic nature of PLs changed starch structure, but it had a greater effect on the structure of alpha-amylase by exposing more tryptophan residues and increasing alpha-helix and beta-sheet contents. Further investigation by using different chain-length fatty acids confirmed the results. The finding in this study is informative to design and fabricate alpha-amylase inhibitors for controlling starch digestion at the molecular level.