The contamination of soils with heavy metals and its associated hazardous effects are a thrust area of today’s research. Rapid industrialization, emissions from automobiles, agricultural inputs, improper disposal of waste, etc., are the major causes of soil contamination with heavy metals. These contaminants not only contaminate soil but also groundwater, reducing agricultural land and hence food quality. These contaminants enter the food chain and have a severe effect on human health. It is important to remove these contaminants from the soil. Various economic and ecological strategies are required to restore the soils contaminated with heavy metals. Phytoremediation is an emerging technology that is non-invasive, cost-effective, and aesthetically pleasing. Many metal-binding proteins (MBPs) of the plants are significantly involved in the phytoremediation of heavy metals; the MBPs include metallothioneins; phytochelatins; metalloenzymes; metal-activated enzymes; and many metal storage proteins, carrier proteins, and channel proteins. Plants are genetically modified to enhance their phytoremediation capacity. In Arabidopsis, the expression of the mercuric ion-binding protein in Bacillus megaterium improves the metal accumulation capacity. The phytoremediation efficiency of plants is also enhanced when assisted with microorganisms, biochar, and/or chemicals. Removing heavy metals from agricultural land without challenging food security is almost impossible. As a result, crop selections with the ability to sequester heavy metals and provide food security are in high demand. This paper summarizes the role of plant proteins and plant–microbe interaction in remediating soils contaminated with heavy metals. Biotechnological approaches or genetic engineering can also be used to tackle the problem of heavy metal contamination.
Salicornia brachiata is an extreme halophyte that grows in salty marshes and is considered to be a potential alternative crop for seawater agriculture. Salicornia seeds are rich in protein, and its tender shoots are eaten as salad greens. Seed storage proteins were fractionated by sequential extraction using different solvents, including distilled water for albumins, NaCl (1.0 M) for globulins, NaOH (0.1 N) for glutelins, and ethanol (70% v/v) for prolamins. Globulins accounted for 54.75% of the total seed storage proteins followed by albumins (34.30%) and glutelins (8.70%). The fractionated proteins were characterized using 2D-diagonal SDS-PAGE and matrix-assisted laser desorption/ionization-time of flight (MALDI-TOF) mass spectrometry. The globulin fraction, composed of seven intermolecular disulfide-linked polypeptide pairs of molecular mass 63.5, 62.5, 54.7, 53.0, 43.2, 38.5, and 35.1 kDa, encompassed a basic and an acidic subunit. Two-dimensional gels revealed approximately 32 spots, with isoelectric points and molecular masses ranging from 4.93 to 11.6 and from ∼5.2 to ∼109.4 kDa, respectively. Protein spots were identified by MALDI-TOF MS peptide mass fingerprint analysis and further classified. Homology analysis demonstrated that 19% of the proteins were involved in metabolism, 16% were involved in signaling, and 15% were regulatory proteins. Peptide mass fingerprint analysis confirmed the presence of inter- and intramolecular disulfide linkages in the globulin fraction. Sulfur-rich proteins are of high nutritional value, and disulfides make S. brachiata a potential source of dietary supplementation.
We describe a series of experiments and numerical simulations that were designed to determine the rate of stress-driven diffusion along interfaces in a damascene copper interconnect structure. Wafer curvature experiments were used to measure the rate of stress relaxation in an array of parallel damascene copper lines, which were encapsulated in a dielectric, and passivated with an overlayer of silicon nitride or silicon carbide. The stress relaxation was found to depend strongly on the choice of passivation. Three-dimensional finite element simulations were used to model the experiments, and showed that this behavior is caused by changes in the diffusivity of the interface between the copper lines and the passivation. By fitting the predicted stress relaxation rates to experimental measurements, we have identified the interfaces that contribute to stress relaxation in the structure, and have estimated values for their diffusion coefficients.
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