RESUMO
BACKGROUND: Germination is considered to improve the nutritive value, antioxidant capacity and functional properties of grains. In this study, changes in the chemical composition, nutritive value and antioxidant capacity of waxy wheat during germination were determined. RESULTS: Over a 48 h period of germination the protein and free lipid contents of germinated waxy wheat were not significantly different from those of the control, whereas the bound lipid content decreased significantly. An increase in levels of ash and dietary fibre was clearly observed for the 48 h-germinated wheat. The total free amino acid content of the 48 h-germinated wheat was 7881 mg kg⻹ flour (dry basis (d.b.)), significantly higher than that of the ungerminated wheat (2207 mg kg⻹ flour, d.b.). In particular, γ-aminobutyric acid increased from 84 mg kg⻹ flour (d.b.) in the control to 155 mg kg⻹ flour (d.b.) in the 48 h-germinated wheat. Germination did not significantly affect the fatty acid composition of both free and bound lipids of waxy wheat, whereas free phenolic compounds increased during germination, resulting in an increase in antioxidant capacity of germinated wheat. CONCLUSION: Germinated waxy wheat had a better nutritional composition, such as higher dietary fibre, free amino acid and total phenolic compound contents, than ungerminated waxy wheat. Therefore germinated waxy wheat should be used to improve the nutritional quality of cereal-based products.
Assuntos
Antioxidantes/análise , Produtos Agrícolas/crescimento & desenvolvimento , Alimento Funcional/análise , Germinação , Sementes/crescimento & desenvolvimento , Triticum/crescimento & desenvolvimento , Aminoácidos/biossíntese , Antioxidantes/metabolismo , Produtos Agrícolas/química , Produtos Agrícolas/metabolismo , Fibras na Dieta/análise , Fibras na Dieta/metabolismo , Farinha/análise , Humanos , Japão , Valor Nutritivo , Fenóis/análise , Fenóis/metabolismo , Sementes/química , Sementes/metabolismo , Triticum/química , Triticum/metabolismoRESUMO
The synthesis of 2-aminobenzenesulfonamide-containing cyclononyne (ABSACN), starting from 2-nitrobenzenesulfonamide and but-2-yne-1,4-diol via Mitsunobu and Nicholas reactions, is described for the development of an adjustable alkyne reagent in click reactions. In a strain-promoted azide-alkyne cycloaddition (SPAAC) reaction, the reactivity of the alkyne is controlled by introducing various N-functionalities. The structure-reactivity relationship is found to be influenced by a transannular hydrogen bond between amino and sulfonyl groups.
RESUMO
BACKGROUND: The 1f1f subtype of the group-specific component (Gc) protein is converted into Gc protein-derived macrophage-activating factor (GcMAF) by enzymatic processing with ß-galactosidase and sialidase. We previously demonstrated that preGc(1f1f)MAF, a full Gc(1f1f) protein otherwise lacking a galactosyl moiety, can be converted to GcMAF by treatment with mouse peritoneal fluid. Here, we investigated the effects of the ß-galactosidase-treated 1s1s and 22 subtypes of Gc protein (preGc(1s1s)MAF and preGc22MAF) on the phagocytic activation of mouse peritoneal macrophages. RESULTS: We demonstrated the presence of Gal-GalNAc disaccharide sugar structures in the Gc(1s1s) protein by western blotting using peanut agglutinin and Helix pomatia agglutinin lectin. We also found that preGc(1s1s)MAF and preGc22MAF significantly enhanced the phagocytic activity of mouse peritoneal macrophages in the presence and absence of mouse peritoneal fluid. CONCLUSION: We demonstrate that preGc(1s1s)MAF and preGc22MAF proteins can be used as effective macrophage activators.
Assuntos
Ativação de Macrófagos/fisiologia , Fatores Ativadores de Macrófagos/metabolismo , Proteína de Ligação a Vitamina D/metabolismo , beta-Galactosidase/metabolismo , Animais , Western Blotting , Humanos , Macrófagos/metabolismo , Camundongos , Fagocitose/fisiologiaRESUMO
BACKGROUND: The 1f1f subtype of the Gc protein (Gc(1f1f) protein) was converted into Gc-derived macrophage-activating factor (GcMAF) by enzymatic processing in the presence of ß-galactosidase of an activated B-cell and sialidase of a T-cell. We hypothesized that preGc(1f1f)MAF, the only Gc(1f1f) protein lacking galactose, can be converted to GcMAF in vivo because sialic acid is cleaved by residual sialidase. Hence, we investigated the effect of preGc(1f1f)MAF on the phagocytic activation of mouse peritoneal macrophages. RESULTS: We examined the sugar moiety of preGc(1f1f)MAF with a Western blot using peanut agglutinin (PNA) and Helix pomatia agglutinin (HPA) lectin. We also found that preGc(1f1f)MAF significantly enhanced phagocytic activity in mouse peritoneal macrophages but only in the presence of the mouse peritoneal fluid; the level of phagocytic activity was the same as that observed for GcMAF. CONCLUSION: PreGc(1f1f)MAF can be used as an effective macrophage activator in vivo.