Phosphorus doped cyanobacterial biochar catalyzes efficient persulfate oxidation of the antibiotic norfloxacin.

In this study, cyanobacterial biochars (CBs) enriched/doped with non-metallic elements were prepared by pyrolysis of biomass amended with different N, S, and P containing compounds. Their catalytic reactivity was tested for persulfate oxidation of the antibiotic norfloxacin (NOR). N and S doping failed to improve CB catalytic reactivity, while P doping increased reactivity 5 times compared with un-doped biochar. Biochars produced with organic phosphorus dopants showed the highest reactivity. Post-acid-washing improved catalytic reactivity. In particular, 950 ℃ acid-washed triphenyl-phosphate doped CB showed the largest degradation rate and reached 79% NOR mineralization in 2 h. Main attributes for P-doped CBs high reactivity were large specific surface areas (up to 655 m2/g), high adsorption, high C-P-O content, graphitic P and non-radical degradation pathway (electron transfer). This study demonstrates a new way to reuse waste biomass by producing efficient P-doped metal-free biochars and presents a basic framework for designing carbon-based catalysts for organic pollutant degradation.

Fast peroxydisulfate oxidation of the antibiotic norfloxacin catalyzed by cyanobacterial biochar.

Peroxydisulfate (PDS) is a common oxidant for organic contaminant remediation. PDS is typically activated by metal catalysts to generate reactive radicals. Unfortunately, as radicals are non-selective and metal catalysts may cause secondary contamination, alternative selective non-radical pathways and non-metal catalysts need attention. Here we investigated PDS oxidation of commonly detected antibiotic Norfloxacin (NOR) using cyanobacterial nitrogen rich biochars (CBs) as catalysts. NOR was fully degraded by CB pyrolysed at 950 °C (CB950) within 120 min. CB950 caused threefold faster degradation than low pyrolysis temperature (PT) CBs and achieved a maximum surface area normalized rate constant of 4.38 × 10-2 min-1 m-2 L compared to widely used metal catalysts. CB950 maintained full reactivity after four repeated uses. High defluorination (82%) and mineralization (>82%) were observed for CB950/PDS. CBs were active over a broad pH range (3-10), but with twice as high rates under alkaline compared with neutral conditions. NOR is degraded by organic, •OH and SO4•- radicals in low PT CBs/PDS systems, where the presence of MnII promotes radical generation. Electron transfer reactions with radicals supplemented dominate high PT CBs/PDS systems. This study demonstrates high PT biochars from algal bloom biomass may find use as catalysts for organic contaminant oxidation.

Modulation of gastrointestinal digestion of ß-lactoglobulin and micellar casein following binding by (-)-epigallocatechin-3-gallate (EGCG) and green tea flavanols.

The effect of binding of flavonoids, (-)-epigallocatechin-3-gallate (EGCG) and green tea extract (GTE), to beta-lactoglobulin (ß-Lg) and micellar casein (micellar casein isolate, MCI) on protein digestibility was investigated. ß-Lg resisted digestion by pepsin, but in the presence of EGCG the digestion of ß-Lg was enhanced. Binding of EGCG to ß-Lg was identified by nitro blue tetrazolium (NBT) staining and found, by isothermal titration calorimetry, to be an enthalpy-driven exothermic process, with a binding constant of 19 950 L mol-1. Binding promoted a more rapid digestion of ß-Lg during simulated upper duodenal digestion. NBT staining indicated a loss of binding of EGCG to ß-Lg during combined gastric and distal small intestinal digestion and correlated with the cleavage of ß-Lg. However, increased ß-Lg heteromer formation and reduced ß-Lg monomer digestibility were observed for the ß-Lg-GTE complex. MCI was more digestible than ß-Lg during pepsin digestion, but reduced digestibility was observed for both MCI-EGCG and MCI-GTE complexes, with loss of binding during intestinal digestion. The free radical scavenging capacity (FRSC) of EGCG remained stable for the ß-Lg-EGCG complex throughout the gastric and intestinal phases of digestion, but this was significantly lowered for the MCI-EGCG complex. These results indicated that polyphenols bind to milk proteins modulating the in vitro digestibility and FRSC of ß-Lg and MCI as a result of the formation of complexes.

Morphology and Structure of Solid Lipid Nanoparticles Loaded with High Concentrations of ß-Carotene.

Solid lipid nanoparticles (SLNs) containing up to 37.5 wt % all-trans ß-carotene in the lipid phase are potential water-dispersible food colorants. SLNs have been made by hot-melt high-pressure homogenization with fully hydrogenated sunflower oil and with polysorbate 80 and sunflower lecithin as stabilizers. Atomic force microscopy revealed the SLNs had thin platelet structures most likely derived from the triglyceride crystal ß-form, as detected by X-ray diffraction. No indications of crystalline ß-carotene were detected. High-performance liquid chromatography analysis showed the extensive isomerization of ß-carotene into more than 10 cis isomers, suggesting that it is present as an amorphous mixture. The high ß-carotene loadings did not affect the triglyceride crystal structure and the morphology of the SLNs. It is suggested the SLNs consist of a platelet core of crystalline triglyceride surrounded by an amorphous ß-carotene-containing layer. The layered structure is suggested to affect the coloring power of the SLNs at ß-carotene loadings above 15 wt % of the lipid phase.

Interactions of coffee and bread crust melanoidins with hydroxycinnamic and hydroxybenzoic acids in aqueous radical environment.

The interactions of coffee and bread crust melanoidins with hydroxycinnamic and hydroxybenzoic acids (HCA/HBA) containing different numbers of -OH and -OCH3 groups localized at different positions on the aromatic ring were investigated. By doing so, mechanism of the interactions was intended to be explained with a structural approach. Experimental studies were carried out in DPPH radical medium. Chemometric methods were used for experimental design and multivariate data analysis. Area under the curve (AUC) values calculated from the plots of time versus inhibition (%) for coffee and bread crust melanoidins and HCA/HBA derivatives were ranged between 6532 ±â€¯97-19,106 ±â€¯85, 3997 ±â€¯102-7565 ±â€¯159 and - 1678 ±â€¯81-22,486 ±â€¯119, respectively. Synergistic interactions were revealed for both coffee and bread crust melanoidins and HCA/HBA derivatives. The significance of the concentrations of coffee and bread crust melanoidins on radical scavenging activity was clearly centered from the scores plots obtained via Principal component analysis (PCA). Phases of radical scavenging reactions were also revealed from the loadings plots.