Hemin has potential application value in plant-based meat analogues. However, mechanisms of interaction between hemin and plant protein are unclear. In this study, soy protein isolate (SPI) was applied to examine these interactions using multi-spectroscopic and molecular docking techniques. Additionally, the influence of hemin on emulsification of SPI was also explored. Fluorescence and UV-Vis spectra showed quenching of SPI by hemin was static, resulting in conformation changes on the surface amino acid residues, around which hydrophobicity was significantly reduced from 425.9 ± 16.2 to 108.9 ± 1.8 (p < 0.05). FTIR and CD spectra results suggested the protein secondary structure altered, and the content of α-helix and random coils increased by 1.13% and 1.43%, respectively. Furthermore, emulsifying properties of SPI were strengthened with increased hemin. This work improves our understanding of interactions between SPI and hemin and offer a theoretical basis for application of heme in plant-based meat analogues.
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| http://dx.doi.org/10.1016/j.foodchem.2023.136183 | DOI Listing |
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