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Bioactives can impact food function either by their dosage or by their forms of dispersion, though the latter remains mostly neglected. Here we report the incidental nanoparticles (iNPs) carrying hepatoprotective bioactives identified in freshwater clam (Corbicula fluminea Muller) soup, which is a folk remedy for liver conditions in East Asia. The soup was fractionated into two iNPs containing fractions with high yield (95.8%) in 35 min by gel chromatography. With hydrodynamic diameter (D h ) range from 40 nm to 149 nm, iNPs were mainly constituted by carbohydrates and proteins. Notably, the majority of bioactives, e.g. taurine (63.2%), ornithine (68.1%) and phytosterols (60.0%), was determined to be carried by the iNPs. It suggested a possible mechanism of elevated delivery and absorption of bioactives, explaining why the clam soup can work at the bioactive concentrations way lower than the individual compound. These iNPs have great potential to be developed into a functional food with most potent nutraceutical effects., Competing Interests: Declaration of competing interest The authors declare no competing financial interest., (Copyright © 2020 Elsevier B.V. All rights reserved.)

Using plant-derived proteins as delivery materials to encapsulate lipophilic bioactive compounds is of great interest. Three protein fractions from brewers' spent grain (BSG) were extracted by the alkaline or alcoholic method with different procedures, and their potential to encapsulate curcumin was evaluated by preparing composite nanoparticles stabilized by lecithin using a pH-cycle method. The three protein fractions showed considerably different encapsulation properties. The particle size and entrapment efficiency varied from 173 to 306 nm and 21.2% to 83.9%, respectively. Compared with the other two fractions, the one extracted with 55% (v/v) ethanol showed better encapsulation performance. Curcumin after encapsulation exhibited an enhanced UV light and thermal stability while its antioxidant activity maintained. These results suggested that BSG protein could be a promising delivery material to encapsulate the water-insoluble bioactive compounds. • Protein fractions were extracted from brewers' spent grain (BSG) by alkaline or alcoholic methods. • Composite nanoparticles were prepared using BSG protein fractions to encapsulate curcumin. • BSG protein fraction obtained by 55% (v/v) ethanol showed better encapsulation performance. • BSG protein improved the UV light and thermal stability of curcumin without receding antioxidant activity. [ABSTRACT FROM AUTHOR]

Licorice was widely used in food and herbal medicine. In its extract industry, a substantial amount of licorice protein was produced and discarded as waste. Herein, we extracted Licorice Protein Isolate (LPI) and explored its potential as a curcumin nanocarrier. Using a pH-driven method, we fabricated LPI-curcumin nanoparticles with diameters ranging from 129.30 ± 3.21 nm to 75.03 ± 1.19 nm, depending on the LPI/curcumin molar ratio. The formation of LPI-curcumin nanoparticles was primarily driven by hydrophobic interactions, with curcumin entrapped in LPI being in an amorphous form. These nanoparticles significantly enhanced curcumin properties in terms of solubility, photochemical stability, and stability under varying pH, storage, and physiological conditions. Moreover, the loaded curcumin exhibited a 2.58-fold increase in cellular antioxidant activity on RAW 264.7 cells and a 1.86-fold increase in antitumor activity against HepG2 cells compared to its free form. These findings suggested that LPI could potentially serve as a promising novel delivery material. [ABSTRACT FROM AUTHOR]

From the aqueous extract of Semen Armeniacae Amarum , a major protein isolate was purified and characterized as a novel member of the 11S globulin family, which is composed of three polypeptides linked by disulfide bond. Furthermore, the feasibility of using the isolated protein for fabricating nanocarriers was investigated. The results indicate that thermal treatment of the globulin induced the rearrangement of the disulfide bond to form homodimers of acid polypeptides during the formation of nanoparticles. The harvested nanoparticles produced by heat-induced assembly are spherical in shape, with an average size of 92 nm and exhibited low cytotoxicity to L-02 and MDCK cell lines. These nanoparticles are capable to encapsulate paclitaxel, estimated the maximum encapsulation efficiency of paclitaxel loaded to the nanoparticles was 92.6% and the maximum release of paclitaxel was 57.4%. This research suggests that the screening of traditional herbal extracts could provide a novel source of protein nanocarriers. Unlabelled Image • A major protein SAP from Semen Armeniacae Amarum was purified and characterized as a novel member of the 11S globulin family. • The nanoparticles were fabricated by thermal treatment of SAP and exhibited low cytotoxicity to L-02 and MDCK cell lines. • Thermal treatment of SAP induced the rearrangement of the disulfide bond to form homodimers of acid polypeptides. • Paclitaxel was successfully encapsulated in the thermal assembled nanoparticles. [ABSTRACT FROM AUTHOR]

Maillard reaction can influence the functionalities of myofibrillar protein (MP). Protein-saccharide Maillard-type conjugates improve the solubility of MP but impair its thermal gelling ability. Besides, the influences of Maillard reaction occurred between reducing sugar and free amino acids on MP were not inspected yet. In this study, arginine-glucose Maillard reaction products (MRPs) were adopted to investigate their effects on the physicochemical and gel properties of chicken MP. The results showed that Arg-Glc MRPs significantly decreased surface hydrophobicity and the content of reactive sulfhydryl group, subsequently influenced the gelling behavior and gel properties, e.g., water holding capacity and gel strength. The dynamic rheological results revealed that MRPs reduced the storage modulus value effectively. Scanning electron microscopy showed that the three-dimensional network structure of MP gel became coarser and irregular by the treatment of Arg-Glc MRPs. These results suggested that Arg-Glc MRPs have influences on both the physicochemical properties and the gel properties of MP, which may provide new information to the effects of MRPs on the water holding capacity and texture of meat products. • MRPs lowered the gel strength and the G′ values of myofibrillar protein (MP). • Arg-Glc MRPs also reduced the surface hydrophobicity and reactive SH group content. • MP gels displayed a coarser and more irregular network by treating with the MRPs. [ABSTRACT FROM AUTHOR]