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 (PGE) 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.

BACKGROUNDOil‐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.RESULTSEmulsions 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.CONCLUSIONSSPIH obtained under HPP could improve the emulsifying and oxidative stability of MP‐prepared O/W emulsions.

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Soybean protein isolate (SPI) is a kind of plant derived protein with high nutritional value, but it is underutilized due to its structural limitations and poor functionalities. This study aimed to investigate the effects of high hydrostatic pressure (HHP) treatment on SPI and sodium alginate (SA) conjugates prepared through the Maillard reaction. The physicochemical properties of the conjugate synthesized under 200 MPa at 60 °C for 24 h (SPI–SA–200) were compared with those of the conjugate synthesized under atmospheric pressure (SPI–SA–0.1), SPI-SA mixture, and SPI. The HHP (200 MPa) significantly hindered the Maillard reaction. This effect was confirmed by performing SDS-PAGE. The alterations in the secondary structures, such as α-helices, were analyzed using circular dichroism spectroscopy and the fluorescence intensity was determined. Emulsifying activity and stability indices of SPI-SA-200 increased by 33.56% and 31.96% respectively in comparison with the SPI–SA–0.1 conjugate. Furthermore, reduced particle sizes (356.18 nm), enhanced zeta potential (‒40.95 mV), and homogeneous droplet sizes were observed for the SPI-SA-200 emulsion. The present study details a practical method to prepare desirable emulsifiers for food processing by controlling the Maillard reaction and improving the functionality of SPI.

We have designed an interactive form of sonification in which the listener navigates through the molecular structures of amino acids over the network of carbon atoms. We use pitch and density as the two main features for the sound design of the four common chemical elements (H, C, N, O). We use multiple concurrently sounding sources to spatially sonify the atoms around a certain carbon atom of the amino acids. The main goal of this paper is to evaluate this sonification approach. We cover the design, execution and evaluation of two separate cycles of experiments that aim to evaluate our sonification approach and get insight in factors that may influence the individual performance of the concurrently sounding source identification and localization.