Subcritical Water Induced Complexation of Soy Protein and Rutin: Improved Interfacial Properties and Emulsion Stability

Abstract

Rutin is a common dietary flavonoid with important antioxidant and pharmacological activities. However, its application in the food industry is limited mainly because of its poor water solubility. The subcritical water (SW) treatment provides an efficient technique to solubilize and achieve the enrichment of rutin in soy protein isolate (SPI) by inducing their complexation. The physicochemical, interfacial, and emulsifying properties of the complex were investigated and compared to the mixtures. SW treatment had much enhanced rutin-combined capacity of SPI than that of conventional method, ascribing to the well-contacted for higher water solubility of rutin with stronger collision-induced hydrophobic interactions. Compared to the mixtures of rutin with proteins, the complex exhibited an excellent surface activity and improved the physical and oxidative stability of its stabilized emulsions. This improving effect could be attributed to the targeted accumulation of rutin at the oil-water interface accompanied by the adsorption of SPI resulting in the thicker interfacial layer, as evidenced by higher interfacial protein and rutin concentrations. This study provides a novel strategy for the design and enrichment of nanovehicle providing water-insoluble hydrophobic polyphenols for interfacial delivery in food emulsified systems.

Enzyme‐assisted development of biofunctional polyphenol‐enriched buckwheat protein: physicochemical properties, in vitro digestibility, and antioxidant activity

“…9 Similar aggregation behavior was found in our previous reports: hydrophobic interactions play a role in the bonding of rutin to the soy protein binary complex. 28 As shown in Table 3, the amino acid composition of buckwheat bran flour is consistent with previous reports. 26 The amino acids are well balanced and are rich in lysine, which is generally the first limiting amino acid in other plant crops.…”

“…), which suggests that the presence of low‐solubility E‐BWP could be related to the presence of a high level of polyphenols, which associated to the protein‐polyphenol conjugates . Similar aggregation behavior was found in our previous reports: hydrophobic interactions play a role in the bonding of rutin to the soy protein binary complex …”

From by‐product to food ingredient: evaluation of compositional and technological properties of olive‐leaf phenolic extracts

“…However, it is important to point out that the emulsions produced were quite vulnerable to physical destabilization phenomena, especially at the highest oil concentration, where it was possible to observe an oily layer on the top of the emulsions soon after the homogenization process. This draws attention on the fact that such phenolic‐rich extracts may be useful when used in combination with other emulsifiers to allow an adequate stabilization of the oil / water interface, as it is was already shown in protein‐stabilized emulsions . Further research therefore has to be carried out to test the efficiency of OLE extracts combined with other food emulsifiers as well as with different homogenization conditions.…”

“…This draws attention on the fact that such phenolic-rich extracts may be useful when used in combination with other emulsifiers to allow an adequate stabilization of the oil / water interface, as it is was already shown in protein-stabilized emulsions. 41 Further research therefore has to be carried out to test the efficiency of OLE extracts combined with other food emulsifiers as well as with different homogenization conditions.…”

Preparation and characterisation of glyceollin‐enriched soya bean protein using solid‐state fermentation

“…The DPPH and ABTS radical scavenging and reducing power were determined (Chen et al ., ). ABTS radical cation (ABTS+) was produced by reacting 7 m m ABTS with 2.45 m m potassium persulphate and stand in the dark for 16 h. The ABTS+ solution was diluted with ethanol ( A 734 nm < 0.70).…”