Preparation and nutritional characterisation of protein concentrate prepared from foxtail millet ().

Plant-based protein sources as a sustainable alternative to animal sources are highly relevant for food and dietary supplements industries. Plant proteins are becoming popular as an eco-friendly source for meeting global protein requirements due to their importance in nutrition, management of metabolic diseases, biological activities, functionality in processed food products and their low carbon footprints. We applied biochemical protein extraction protocol and prepared protein concentrate from an underutilised cereal, foxtail millet, with plausible applications in foods and supplements.

Peroxiredoxin-6: A Guardian of Lung Pathophysiologies.

The moonlighting protein, Prdx-6, exhibits peroxidase activity, phospholipase activity, and lysophosphatidylcholine acyltransferase (LPCAT) activity. Although it is ubiquitous in expression, its level is prominently high in the lung. Prdx-6 has been known to be an important enzyme for the maintenance of normal lung physiologies including, anti-oxidant defense, lung surfactant homeostasis, and cell signaling.

pH induced conformational alteration in human peroxiredoxin 6 might be responsible for its resistance against lysosomal pH or high temperature.

Peroxiredoxin 6 (Prdx6), the ubiquitously expressed enzyme belonging to the family of peroxidases, namely, peroxiredoxins, exhibits a unique feature of functional compartmentalization within cells. Whereas, the enzyme localized in cytosol shows glutathione peroxidase activity, its lysosomal counterpart performs calcium independent phospholipase A2 (aiPLA2) activity. Like any true moonlighting protein, these two activities of Prdx6 are mutually exclusive of each other as a function of the pH of the cellular compartments.

Structural basis of peroxidase catalytic cycle of human Prdx6.

Peroxiredoxin 6 (Prdx6) is a ubiquitously expressed antioxidant non-selenium glutathione peroxidase that is known to play a major role in various physiological and pathological processes. It belongs to the family of peroxidases (referred to as Peroxiredoxins, Prdx's) that work independently of any prosthetic groups or co-factors, and instead utilize a peroxidatic thiol residue for peroxide reduction. Mammalian Prdx's are classified according to the number of Cys implicated in their catalytic activity by the formation of either inter-molecular (typical 2-Cys, Prdx1-4) or intra-molecular (atypical 2-Cys, Prdx5) disulfide bond, or non-covalent interactions (1-Cys, Prdx6).

The anti-oxidant enzyme, Prdx6 might have cis-acting regulatory sequence(s).

Peroxiredoxin 6 (Prdx6) is a ubiquitously expressed 1-cysteine Peroxiredoxin found throughout all phyla. In mammals, under different physiological conditions, it has evolved from a peroxidase to a multifunctional enzyme. Among the mammalian Prdx6's, human and rat Prdx6's are the most extensively studied.

Hyperoxidation of Peroxiredoxin 6 Induces Alteration from Dimeric to Oligomeric State.

Peroxiredoxins(Prdx), the family of non-selenium glutathione peroxidases, are important antioxidant enzymes that defend our system from the toxic reactive oxygen species (ROS). They are thiol-based peroxidases that utilize self-oxidation of their peroxidatic cysteine (C) group to reduce peroxides and peroxidized biomolecules. However, because of its high affinity for hydrogen peroxide this peroxidatic cysteine moiety is extremely susceptible to hyperoxidation, forming peroxidase inactive sulfinic acid (Cys-SO₂H) and sulfonic acid (Cys-SO₃H) derivatives.

Macromolecular crowding: Macromolecules friend or foe.

Background: Cellular interior is known to be densely crowded due to the presence of soluble and insoluble macromolecules, which altogether occupy ~40% of the total cellular volume. This results in altered biological properties of macromolecules.

Scope Of Review: Macromolecular crowding is observed to have both positive and negative effects on protein folding, structure, stability and function.