Effects of Different Biochars,Activated Carbons and Redmuds on the Growth of Trifolium repens and As and Pb Stabilization in a Former Mine Technosol

Soil pollution by metal(loid)s is an important issue in Europe, as it causes environmental and health problems. Therefore, remediation of these areas is needed. The success of phytoremediation process will depend on the ability of plants to implement, which can require the addition of amendments to the soil in order to improve soil conditions, immobilize pollutant and thus ameliorate plant growth. Amendments that can be used are biochar, activated carbon and redmuds, all of which have previously shown positive outcomes. The objectives of this study were to evaluate the effects of several amendments (biochars, activated carbons and redmuds) on (i) the soil physico-chemical properties of a former mine technosol contaminated by As and Pb, (ii) As and Pb immobilization and (iii) the growth of Trifolium repens. Results showed that amendment addition could ameliorate soil conditions, by reducing soil acidity (pH increased by 1.2 to 1.7 units) and immobilizing pollutants (85 to 99% of Pb immobilized); and improve plant growth (dry weight increased 1.5 to 2.5 times). However, not all amendments were beneficial to the soil and plant. For instance, the L27 activated carbon acidified soil pH, mobilized As and lowered plant growth. This study has allowed us to conclude that amendment effect is dependent on soil type, metal(loid)s and amendment properties, and it is thus necessary to choose the right amendment. Finally, amendments could be combined for better outcomes.

     

Use of porcine fibrinogen as a model glycoprotein to study the binding specificity of the three variants of K88 lectin.

Known glycoproteins were used to determine the differences occurring in the binding specificities of the three variants of the K88 lectin in an approach essentially based on lectin blotting. During the screening, it was demonstrated that each variant of the K88 lectin biotinylated via its amino groups (NbioK88) exhibited a characteristic binding to the three chains of porcine fibrinogen. NbioK88ab weakly bound to A alpha chains, NbioK88ac bound to B beta and gamma chains, and NbioK88ad bound only to the gamma chain. To validate this model, the oligosaccharide moieties of porcine fibrinogen were analyzed with glycosidases and by lectin blotting and sugar composition. Both the B beta chain and gamma chain carry biantennary N-glycans of the N-acetyllactosamine type that are not recognized by K88 lectins. A alpha chains are substituted by sialylated T antigen. O-glycans were also detected on B beta and gamma chains of porcine fibrinogen and contribute to the recognition of these chains by K88ac and K88ad fimbriae.