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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.)

Leguminous plants have formed a popular subject of research owing to the abundance of proteins and peptides with important biological activities that they produce. The antifungal proteins and peptides have been purified from a number of leguminous species. However, research continues to discover novel antifungal plant-produced peptides and proteins are being needed, specially those novel ones with both antifungal activity and other significant bioactivities. The objective of this study was to isolate a novel peptide from Phaseolus limensis. A 6.8 kDa peptide designated Limyin, with both antifungal and antiproliferative activity, was isolated from the large lima bean ( P. limensis) legumes. The isolation procedure consisted of extraction, precipitation, affinity chromatography on Affi-gel blue gel, ion chromatography on SP-Toyopearl, and gel filtration on Superdex 75. Its N-terminal sequence was determined to be KTCENLATYYRGPCF, showing high homology to defensin and defensin precursors from plants. It potently suppressed mycelial growth in Alternaria alternata, Fusarium solani, and Botrytis cinerea. Its antifungal activity was stable up to 80°C. It showed antiproliferative activity towards tumor cells including human liver hepatoma cells Bel-7402 and neuroblastoma cells SHSY5Y. However, it had no effect on bacteria Staphylococcus aureus and Salmonella. The present findings make a significant addition of the research on leguminous plants. [ABSTRACT FROM AUTHOR]

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]

Abstract: Multiple bradykinin-related peptides including a novel bradykinin structural variant, (Val1)-bradykinin, have been identified from the defensive skin secretion of Guenther''s frog, Hylarana guentheri by a tandem mass spectrometry method. Subsequently, four different preprobradykinin cDNAs, which encoded multiple bradykinin copies and its structural variants, were consistently cloned from a skin derived cDNA library. These preprobradykinin cDNAs showed little structural similarity with mammalian kininogens and the kininogens from the skin of toads, but have regions that are highly conserved in the kininogens from another ranid frog, Odorrana schmackeri. Alignment of these preprobradykinins revealed that preprobradykinin 1, 2 and 3 may derive from a single gene by alternative exon splicing. [Copyright &y& Elsevier]

Abstract: Brevinins are peptides of 24 amino acid residues, originally isolated from the skin of the Oriental frog, Rana brevipoda porsa, by nature of their microbicidal activity against a wide range of Gram-positive and Gram-negative bacteria and against strains of pathogenic fungi. cDNA libraries were constructed from lyophilized skin secretion of three, unstudied species of Chinese frog, Odorrana schmackeri, Odorrana versabilis and Pelophylax plancyi fukienensis, using our recently developed technique. In this report, we describe the “shotgun” cloning of novel brevinins by means of 3′-RACE, using a “universal” degenerate primer directed towards a highly conserved nucleic acid sequence domain within the 5′-untranslated region of previously characterized frog skin peptide cDNAs. Novel brevinins, deduced from cloned cDNA open-reading frames, were subsequently identified as mature peptides in the same samples of respective species skin secretions. Bioinformatic analysis of both prepro-brevinin nucleic acid sequences and translated open-reading frame amino acid sequences revealed a highly conserved signal peptide domain and a hypervariable anti-microbial peptide-encoding domain. The experimental approach described here can thus rapidly provide robust structural data on skin anti-microbial peptides without harming the donor amphibians. [Copyright &y& Elsevier]

Structural homologues of vertebrate regulatory peptides found in defensive skin secretions of anuran amphibians often display enhanced bioactivity and receptor binding when compared with endogenous mammalian peptide ligands. Maximakinin, a novel N-terminally extended bradykinin (DLPKINRKGPRPPGFSPFR) from the skin venom of a Chinese toad (Bombina maxima), displays such activity enhancement when compared with bradykinin but is additionally highly selective for mammalian arterial smooth muscle bradykinin receptors displaying a 50-fold increase in molar potency in this smooth muscle type. In contrast, a 100-fold decrease in molar potency was observed at bradykinin receptors in intestinal and uterine smooth muscle preparations. Maximakinin has thus evolved as a “smart” defensive weapon in the toad with receptor/tissue selective targeting. Natural selection of amphibian skin venom peptides for antipredator defence, through inter-species delivery by an exogenous secretory mode, produces subtle structural stabilisation modifications that can potentially provide new insights for the design of selectively targeted peptide therapeutics. [Copyright &y& Elsevier]