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The influences of soy protein isolate hydrolysate (SPIH) obtained during different pressure treatments for 4 h on pasting and short-term retrogradation behaviors of maize starch (MS) were investigated. The results showed solubility of MS markedly increased, whereas swelling power decreased with increased SPIH concentration and pressure. Compared with native MS, the addition of SPIH led to decrease of peak viscosity, final viscosity, setback, and breakdown, whereas pasting temperature was increased. Meanwhile, differential scanning calorimetry (DSC) analysis also showed an increase in gelatinization temperature. In addition, low-field nuclear magnetic resonance (LF-NMR) analysis indicated that the tight association of water and starch molecules was observed with increasing pressures and additions of SPIH. Confocal laser scanning microscopy (CLSM) and atomic force microscope (AFM) images indicated that SPIH obtained at 200 MPa dispersed in the MS gel system to block the formation of hydrogen bonds and inhibit the recrystallization of MS. Fourier transform infrared (FTIR) spectroscopy analysis demonstrated that the addition of SPIH resulted in a decrease in hydrogen bonds within the starch molecules and the result supported above CLSM and AFM measurement results. The results proved that the addition of SPIH could effectively influence pasting characteristics and inhibit the short-term retrogradation of MS, which can be helpful to the application of SPIH in starch-based functional foods.

The molecular interactions and mechanisms between four ethyl esters (ethyl acetate, ethyl butyrate, ethyl hexanoate, and ethyl octanoate) and myofibrillar proteins (MPs) were investigated. The gas chromatography and mass spectrometry results showed that binding capability was significantly enhanced as MP concentrations increased (p ethyl hexanoate > ethyl butanoate > ethyl acetate (p

Background Oil-in-water (O/W) emulsions are thermodynamically unstable and are easily oxidized. Recently, protein hydrolysates have been used to enhance the emulsifying and oxidative stability of emulsions. High-pressure processing (HPP) enzymatic hydrolysates of soy protein isolate have higher bioactivities. The objective of the study was to investigate the effects of various soy protein isolate hydrolysate (SPIH) concentrations obtained during different 4 h pressure treatments on improving the emulsifying and oxidative stability of myofibrillar protein (MP) emulsions. Results Emulsions with 4 mg mL-1 SPIH obtained at 200 MPa had the highest emulsifying activity index and emulsion stability index (P ≤ 0.05). This increase in emulsion stability was related to increased zeta potential and reduced average particle size. Optical microscopy and confocal laser scanning microscopy observations confirmed that emulsions with 4 mg mL-1 SPIH possessed relatively small oil droplets. The addition of SPIH obtained at 200 MPa significantly reduced thiobarbituric acid reactive substance values (P ≤ 0.05) of emulsions during 8 days of storage. Concurrently, the carbonyl content remained the lowest and the sulfhydryl content remained the highest, which indicated that the emulsions had higher protein oxidative stability. Conclusions SPIH obtained under HPP could improve the emulsifying and oxidative stability of MP-prepared O/W emulsions.

Enzymatic hydrolysis of soy protein isolate by Corolase PP under high hydrostatic pressure conditions was studied and the effects of hydrolysis on antioxidant and antihypertensive activities were investigated. As observed, high hydrostatic pressure (80-300MPa) enhanced the hydrolytic efficiency of Corolase PP and decreased the surface hydrophobicity of the hydrolysates. Hydrolysates obtained at 200MPa for 4h had higher bioactivities (reducing power, ABTS radical-scavenging and ACE inhibitory activities). The molecular weight (MW) determination indicated that hydrolysis at high hydrostatic pressure could increase the production of small peptides (3kDa) and the amino acid sequences of these peptides with different inhibitory abilities, less than 3kDa, in hydrolysates were identified using matrix-assisted laser desorption/ionization time of flight mass spectrometry (MALDI TOF MS). These results indicated that high hydrostatic pressure combined with Corolase PP treatments could be used as a potential technology to produce bioactive peptides from soy protein isolate.

Sea buckthorn has long been used as a functional food to regulate cholesterol, relieve angina, and diminish inflammation. Flavonoids are one of the main active components in sea buckthorn. We investigated the effects of sea buckthorn flavonoid (SF) treatment on two pathways that mediate inflammation, the mitogen-activated protein kinase (MAPK) and nuclear factor-kappa B (NF-κB) pathways, to explore the anti-inflammatory activity of SFs in lipopolysaccharide (LPS)-stimulated RAW264.7 macrophages. The LPS-induced over-production of nitric oxide (NO) and prostaglandin E2 (PGE2) was inhibited by SFs through a mechanism related to the modulatory effects of the inducible nitric oxide synthase (iNOS) and cyclooxygenase-2 (COX-2) genes. Additionally, SFs downregulated the production and mRNA expression of pro-inflammatory cytokines including tumor necrosis factor (TNF)-α, interleukin (IL)-6 and IL-1β. Moreover, SFs inhibited the phosphorylation of the p38 and stress-activated protein kinase/jun amino-terminal kinase (SAPK/JNK) MAPK pathways, and they reduced the nuclear translocation of NF-κB to prevent its activation by blocking the phosphorylation and degradation of inhibitor protein of NF-κB α (IκB-α). Based on these findings, SFs may exert their inhibitory effects on inflammation by regulating the release of inflammatory mediators through the MAPK and NF-κB pathways. SFs highlight the potential benefits of using functional foods with anti-inflammatory actions to combat inflammatory diseases.