Type I (Complex I) and type II nanocomplexes (Complex II) were created in this work for curcumin (Cur) delivery using ovalbumin (OVA, 1.0% w/w) and sodium alginate (ALG, 0.5% w/w) as building blocks. OVA was heated at 90 °C for 5 min at pH 7.0 and then coated with ALG at pH 4.2 to produce Complex I; OVA−ALG electrostatic complex was created at pH 4.0, which was treated at 90 °C for 5 min thereafter yielding Complex II. Complex I presented an irregular elliptical shape with a diameter of ∼250 nm, whereas Complex II adopted a defined spherical structure of a smaller size (∼200 nm). Complex II did not dissociate at the pH range of 5−7, which was different from Complex I. Cur was loaded into the nonpolar matrix of nanocomplexes through hydrogen bonding and hydrophobic interactions, and Complex II displayed a higher loading capacity than Complex I. Nanocomplexes were resistant to pepsinolysis during simulated gastrointestinal digestion, which enhanced the stability and controlled release of loaded Cur, thereby improving Cur bioaccessibility from ∼20% (free form) to ∼60%. Additionally, nanocomplexes contributed to the cellular antioxidant activity (CAA) of Cur by promoting its cellular uptake. The CAA of Cur was also better preserved in nanocomplexes especially in Complex II after digestion owing to the increased stability and bioaccessibility. Results from this work highlighted the effect of nanocomplex encapsulation on the performance of Cur and revealed the critical role of preparation method in the physicochemical attributes of nanocomplexes.
The protein subunit is the most important basic unit of protein, and its study can unravel the structure and function of seed storage proteins in faba bean. In this study, we identified six specific protein subunits in Faba bean (cv. Qinghai 13) combining liquid chromatography (LC), liquid chromatography-electronic spray ionization mass (LC-ESI-MS/MS) and bio-information technology. The results suggested a diversity of seed storage proteins in faba bean, and a total of 16 proteins (four GroEL molecular chaperones and 12 plant-specific proteins) were identified from 97-, 96-, 64-, 47-, 42-, and 38-kD-specific protein subunits in faba bean based on the peptide sequence. We also analyzed the composition and abundance of the amino acids, the physicochemical characteristics, secondary structure, three-dimensional structure, transmembrane domain, and possible subcellular localization of these identified proteins in faba bean seed, and finally predicted function and structure. The three-dimensional structures were generated based on homologous modeling, and the protein function was analyzed based on the annotation from the non-redundant protein database (NR database, NCBI) and function analysis of optimal modeling. The objective of this study was to identify the seed storage proteins in faba bean and confirm the structure and function of these proteins. Our results can be useful for the study of protein nutrition and achieve breeding goals for optimal protein quality in faba bean.
Faba bean (Vicia faba L.), a partially allogamous species, is rich in protein. Condensed tannins limit the use of faba beans as food and feed. Two recessive genes, zt-1 and zt-2, control the zero tannin content in faba bean and promote a white flower phenotype. To determine the inheritance and develop a linkage map for the zt-1 gene in the faba bean germplasm M3290, F 2 and F 3 progenies were derived from the purple flower and high tannin content genotypes Qinghai12 and zt-1 line M3290, respectively. Genetic analysis verified a single recessive gene for zero tannin content and flower colour. In total, 596 SSR markers and 100 ISSR markers were used to test the polymorphisms between the parents and bulks for the contrasting flower colour via Bulked Segregant Analysis (BSA). Subsequently, six SSR markers and seven ISSR markers were used to genotype the entire 413 F 2 population. Linkage analysis showed that the zt-1 gene was closely linked to the SSR markers SSR84 and M78, with genetic distances of 2.9 and 5.8 cM, respectively. The two flanked SSR markers were used to test 34 faba bean genotypes with different flower colours. The closely linked SSR marker SSR84 predicted the zt-1 genotypes with absolute accuracy. The results from the marker-assisted selection (MAS) from this study could provide a solid foundation for further faba bean breeding programmes.
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