No abstract

Environmental benefits reported in the literature of using biochar as a soil amendment are generally increased microbial activity and reduced greenhouse gas (GHG) emissions. This study determined the effects of amendment with biomass feedstocks (spent coffee grounds, wood pellets, and horse bedding compost) and that of biochars (700°C) produced from these feedstocks on soil microbial biomass (C and N) and activity. Soils were amended with these substrates at 0.75% by weight and incubated for up to 175 d under laboratory conditions. Biochar residual effects on soil microbial activity were also studied by amending these soils with either ammonium nitrate (NHNO, 35 mg N kg) or with glucose (864 mg C kg) plus NHNO. Soil microbial biomass C and N, net N mineralization, and CO, NO, and CH emissions were measured. Amendment with biomass feedstocks significantly increased soil microbial biomass and activity, whereas amendment with the biochars had no significant effect. Also, biochar amendment had no significant effect on either net N mineralization or NO and CH emissions from soil. These results indicate that production of biochars at this high temperature eliminated potential substrates. Microbial biomass C in biochar-amended and unamended soils was not significantly different following additions of NHNO or glucose plus NHNO, suggesting that microbial access to otherwise labile C and N was not affected. This study shows that biochars produced at 700°C, regardless of feedstock source, do not enhance soil microbial biomass or activity.

There have been limited studies of how pyrolysis temperature and activation processes alter the chemical properties of biochar and how these changes influence ammonium (NH), nitrate (NO), and phosphate (PO) sorption. This study compared the chemical properties of biochars and activated biochars (ActBC with steam and CO activation) produced by slow pyrolysis at 200 (BC200), 400 (BC400), 600 (BC600), 800 (ActBC200, ActBC400, ActBC600), and 850°C (sulfachar-S enriched biochar with steam activation). Quantitative solid-state C nuclear magnetic resonance spectroscopy and elemental analysis were used to study temperature and activation on biochar chemical properties. The sorption capacity of biochars for NH, NO, and PO were measured by batch sorption experiments. Nuclear magnetic resonance spectroscopy data showed that BC200 contained mainly aliphatic C compounds (86% of O-alkyl) belonging to cellulose and hemicellulose, whereas BC400 and BC600 composition was dominated by fused aromatic C structures, containing 81 and 97% aromatic C, respectively. Increasing pyrolysis temperatures decreased biochar total C but increased its cation exchange capacity, pH, and contents of total N and P, calcium, potassium, and magnesium. The BC200 released NO and PO, whereas sulfachar and ActBC200 sorbed significantly higher amounts NO and PO than BC600 by 83 and 96%, respectively, across aqueous solutions. Sulfachar and BC400 sorbed significantly greater amounts NH than did the other biochars. This study shows that production temperature significantly affects biochar chemical properties and that activation increases NO and PO sorption. These results suggest that activated biochar could be useful for sorbing soil N and P, thereby reducing leaching losses.

There is a need to develop reliable methods to assess the safety of genetically modified and other novel foods. The aim of this study was to identify protein biomarkers of food allergy in mice exposed to ovomucoid (OVM), a major food allergen found in chicken egg white. BALB/c mice were repeatedly sensitized by gavage with OVM and cholera toxin (CT) and control mice were exposed to a mixture of amino acids with CT. At the endpoint, all mice were challenged intraperitoneally with OVM and alum. Type-1 hypersensitivity was confirmed in OVM-sensitized mice by observation of clinical signs of anaphylaxis and elevated levels of plasma histamine, OVM-specific IgE and OVM-specific IgG by ELISA. Differential protein expression was assessed in albumin-depleted plasma as well as in mesenteric lymph node, liver, spleen, and ileum by two-dimensional difference gel electrophoresis (2D-DIGE). Differentially expressed proteins were identified by liquid chromatography with tandem mass spectrometry. Plasma proteins overexpressed in OVM-sensitized mice included haptoglobin (41-fold), serum amyloid A (19-fold) and peroxiredoxin-2 (1.9-fold). Further validation of these plasma proteins in other animal models of food allergy with different food allergens is required to assess their potential as candidate biomarkers for use in evaluating the allergenicity of novel foods.