摘要
Food protein fibrils are progressively recognized as promising matrixes for the preservation and delivery of bioactive compounds. In this study, soy protein fibrils (SPF) formed at 4, 8, and 12 h (80 degrees C, pH 2.0) were utilized as carriers to complex with curcumin at pH 3.2. SPF with extreme aspect ratios exhibited a higher surface hydrophobicity compared to soy protein isolate (SPI), which improved its ability to form soluble complexes with curcumin. However, a prolonged heating time of 12 h decreased the surface hydrophobicity of SPF since the formation of compact fibrillar aggregates. Further experiments revealed SPF8 (heated for 8 h) had a higher affinity for curcumin, and its predominant interactions were hydrophobic interaction and hydrogen bonding. The curcumin solubility of SPF8-Cur (405.7 mu g/mL) significantly enhanced compared to that of SPI-Cur (95.6 mu g/mL) at the ratio (protein/fibril to curcumin) of 12.5. The DPPH center dot and ABTS center dot+ scavenging capacities of the SPF8-Cur complex were each roughly 1.7 and 2.7 times greater than those of free curcumin. Moreover, SPF8-Cur complex presented excellent antioxidant and outstanding sustained-release properties, further offering opportunities for the release of curcumin in the intestine and improving the bioaccessibility and bioavailability of curcumin.