ascorbic-acid and hydrogen-sulfite

The impact of glycosylation on anthocyanin stability has largely been associated with sugar type, site, and size, with glycosyl stereochemistry being under-explored. Seven cyanidin-3-glycosides were isolated by HPLC, diluted in pH 1-9, mixed with bisulfite or ascorbic acid at pH 3, and stored for 8 weeks (25 °C, dark). Spectral changes, half-lives, and bleaching rates were determined. Cyanidin-3-galactoside was more reactive (susceptible to hydration and bleaching) than cyanidin-3-glucoside. The 1 → 2 disaccharides exhibited greater λ

Topics: Anthocyanins; Ascorbic Acid; Chromatography, High Pressure Liquid; Galactosides; Glycosides; Glycosylation; Half-Life; Hydrogen-Ion Concentration; Morus; Sulfites

Effects of oxidative browning inhibitors on sweet potato protein (SPP) recovery and quality were studied. Oxidative browning inhibitors successfully decreased sweet potato oxidative browning, but reduced both SPP extractability and recovery. Ultrafiltration/diafiltration processed sweet potato (UDSP) protein (at pH 4, 6 and 7) showed significantly (p<0.05) higher yield, purity, solubility, thermal stability and amino acid constituents than that of isoelectrically precipitated sweet potato (IPSP) protein (at pH 4). The yield of UDSP proteins was more than twice that of IPSP protein. Denaturation temperature (Td), enthalpy change (ΔH) and solubility (at pH 3 and 8) of UDSP proteins were in the ranges 82.89-90.29 °C, 6.34-11.35 (J/g) and 71.4-94.2%, respectively, while that of IPSP protein were 85.27 °C, 2.35 (J/g) 31.2% and 55.5%, respectively. Ratio of SPP essential amino acid to the total amino acid ratio ranged from 0.49 to 0.51. SPP in vitro digestibility and digestibility-corrected amino acid score (PDCAAS) ranged 70-80.7% and 44.79-51.08%, respectively.

Topics: Amino Acids; Ascorbic Acid; Citric Acid; Ipomoea batatas; Oxidation-Reduction; Pigmentation; Plant Proteins; Protein Stability; Solubility; Sulfites; Temperature; Thermodynamics; Ultrafiltration

Tryptophan 2,3-dioxygenase (TDO) is the first enzyme in the tryptophan oxidation pathway. It is a hemoprotein and its heme prosthetic group is present as a heme-ferric (heme-Fe(3+)) form that is not active. To be able to oxidize tryptophan, the heme-Fe(3+) form of the enzyme must be reduced to a heme-ferrous (heme-Fe(2+)) form and this study describes conditions that promote TDO activation. TDO is progressively activated upon mixing with tryptophan in a neutral buffer, which leads to an impression that tryptophan is responsible for TDO activation. Through extensive analysis of factors resulting in TDO activation during incubation with tryptophan, we conclude that tryptophan indirectly activates TDO through promoting the production of reactive oxygen species. This consideration is supported by the virtual elimination of the initial lag phase when either pre-incubated tryptophan solution was used as the substrate or a low concentration of superoxide or hydrogen peroxide was incorporated into the freshly tryptophan and TDO mixture. However, accumulation of these reactive oxygen species also leads to the inactivation of TDO, so that both TDO activation and inactivation proceed with the specific outcome depending greatly on the concentrations of superoxide and hydrogen peroxide. As a consequence, the rate of TDO catalysis varies depending upon the proportion of the active to inactive forms of the enzyme, which is in a dynamic relationship in the reaction mixture. These data provide some insight towards elucidating the molecular regulation of TDO in vivo.

Topics: Aedes; Animals; Ascorbic Acid; Enzyme Activation; Hydrogen Peroxide; Kynurenine; Oxidants; Recombinant Proteins; Reducing Agents; Spectrophotometry, Ultraviolet; Sulfites; Superoxides; Tryptophan; Tryptophan Oxygenase