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• Inhibition of starch digestion in nonionic steric emulsifier Pluronics was explored. • The role of hydrophobic domain of both α-amylase and substrates was disclosed. • Pluronic causes more changes in amylase structure than it affects starch structure. • Design of amylase inhibitors can be considered from changing hydrophobic groups. 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. [ABSTRACT FROM AUTHOR]