Molecular Food Science Laboratory, College of Food & Biology Engineering, Zhejiang Gongshang University, Hangzhou 310018, China.
Molecular Food Science Laboratory, College of Food & Biology Engineering, Zhejiang Gongshang University, Hangzhou 310018, China.
Food Chem. 2021 Mar 30;341(Pt 1):128211. doi: 10.1016/j.foodchem.2020.128211. Epub 2020 Sep 28.
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 α-amylase by exposing more tryptophan residues and increasing α-helix and β-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 α-amylase inhibitors for controlling starch digestion at the molecular level.
淀粉消化的理化机制非常复杂，因为它可能受到淀粉酶抑制剂与底物或酶的非价相互作用的影响。疏水相互作用在淀粉消化过程中的作用尚不清楚。在这项研究中，使用具有不同疏水性的聚轮烷（PLs）作为模型两亲性化合物，通过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结构，但通过暴露更多色氨酸残基并增加α-螺旋和β-折叠含量，对α-淀粉酶的结构有更大的影响。使用不同链长的脂肪酸进行进一步研究证实了这一结果。本研究的发现为设计和制备用于控制淀粉消化的α-淀粉酶抑制剂提供了有价值的信息，有助于在分子水平上控制淀粉消化。
