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Physical interactions often occur between major food components during food processing. These interactions may involve starch, lipids, and proteins forming V-type starch-lipid complexes or ternary starch-lipid-protein complexes of larger molecular size and greater structural order. Complexes between starch and lipids have been the subject of intensive research for over half a century, whereas the study of starchlipid-protein complexes is a relatively new field with only a limited amount of knowledge being gained so far. The formation of these complexes can significantly affect the functional and nutritional properties of finished food products in terms of flavor, texture, shelf life, and digestibility. This article provides a comprehensive review of starch-lipid and starch-lipid-protein complexes, including their classification, factors affecting their formation and structure, and preparative and analytical methods. The review also considers how complexes affect the physicochemical and functional properties of starch, including digestibility, and potential applications in the food industry. K E Y W O R D Sapplications, digestibility, multi-scale structure, preparative methods, starch-lipid complex, starch-lipidprotein complex 1056

The aim of the present study was to investigate the interactions between maize starch (MS), β-lactoglobulin (βLG), and monoglycerides (MG) containing different fatty acids in a model system. Results from the Rapid Visco Analyzer (RVA) showed that MS–MGC14:0 and MS–MGC16:0 systems presented a viscosity peak during the RVA cooling and/or holding stage, while MS–MGC18:0, MS–MGC18:1, and MS–MGC18:2 systems did not show obvious changes in the pasting profile. Addition of βLG altered significantly the pasting profiles of MS–MG systems in different ways, with the most obvious change observed for the MS–MGC18:0 system. Results from differential scanning calorimetry (DSC), Raman spectroscopy, and X-ray diffraction showed that the complexes in ternary systems were more ordered than those in binary systems. The thermal transition temperatures of complexes in binary and ternary systems were similar, although the enthalpy changes were greater for ternary than for binary systems. From the above results, we concluded that addition of βLG promoted the formation of MS–MG complexes rather than the involvement of formation of ternary MS–MG−βLG complexes.

The two major intracellular protein degradation systems, the ubiquitin-proteasome system (UPS) and autophagy, work collaboratively in many biological processes including development, apoptosis, aging, and countering oxidative injuries. We report here that, in human retinal pigment epithelial cells (RPE), ARPE-19 cells, proteasome inhibitors, clasto-lactacystinβ-lactone (LA) or epoxomicin (Epo), at non-lethal doses, increased the protein levels of autophagy-specific genes Atg5 and Atg7 and enhanced the conversion of microtubule-associated protein light chain (LC3) from LC3-I to its lipidative form, LC3-II, which was enhanced by co-addition of the saturated concentration of Bafilomycin A1 (Baf). Detection of co-localization for LC3 staining and labeled-lysosome further confirmed autophagic flux induced by LA or Epo. LA or Epo reduced the phosphorylation of the protein kinase B (Akt), a downstream target of phosphatidylinositol-3-kinases (PI3K), and mammalian target of rapamycin (mTOR) in ARPE-19 cells; by contrast, the induced changes of autophagy substrate, p62, showed biphasic pattern. The autophagy inhibitor, Baf, attenuated the reduction in oxidative injury conferred by treatment with low doses of LA and Epo in ARPE-19 cells exposed to menadione (VK3) or 4-hydroxynonenal (4-HNE). Knockdown of Atg7 with siRNA in ARPE-19 cells reduced the protective effects of LA or Epo against VK3. Overall, our results suggest that treatment with low levels of proteasome inhibitors confers resistance to oxidative injury by a pathway involving inhibition of the PI3K-Akt-mTOR pathway and activation of autophagy.

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