In recent years, the effects of fluoride (F) pollution in numerous ecosystems such as groundwater, soil, etc. Have become a major issue worldwide. This increase in F pollution is a direct consequence of the unbridled use of fertilizers in agricultural and several other human activities that require immediate and appropriate action. Therefore, this manuscript reveals important findings on the efficacy of bacteria isolated from agricultural fields in central Chhattisgarh in manifesting resistance to F and in reversing the F-induced oxidative damage in susceptible Oryza sativa L, (Var. MTU1010). Chronic exposure of Oryza sativa L. to sodium fluoride (NaF) (50 mg L- 1) severely impeded growth and various physiological parameters such as germination percentage, biomass and root and shoot length and stimulated the formation of reactive oxygen species (ROS), which enhanced electrolyte leakage and formation of cytotoxic products like malondialdehyde. To this end, potential bacterial strains, namely MT2A, MT3A, MT4A, and Du3A were isolated, screened for various plant growth promoting (PGP) traits and used to explore their efficiency to mitigate F toxicity in Oryza sativa L. in vivo. The seedlings inoculated with the bacterial strains showed significant development as evidenced by an increase in root and shoot length, biomass and chlorophyll content. Additionally, inoculation of these strains in combination with F stress significantly decreased oxidative stress by increasing the expression of protective genes encoding antioxidant enzymes and boosted agronomic traits remarkably. Overall, the manuscript demonstrates the pivotal role played by the isolated bacteria in abating ill effects of F in the Oryza sativa L. seedlings and proves their potential as protective bioagents against F stress.

Psychrophiles are cold-adapted microorganisms living in cold regions and are known to generate cold-active enzymes such as proteases, lipases, and peptidases. These types of enzymes are a major part of the market of the food and textile sector. This study aimed to isolate and characterize the cold-active and detergent-stable, extracellular protease from psychotrophic bacteria Serratia sp. TGS1 (OQ654005). Protease was purified by gel permeation chromatography using Sephadex G-75. The specific activity of the purified protease was 250 U/mg at 15 & DEG;C, with a purification fold of 5.68 and a percentage yield of 60%. The cold active protease was stable within a temperature range of 5-30 & DEG;C and a pH range of 6-10. Ca+2 and Mg+2 enhanced its activity while chelators like ethylenediaminetetraacetic acid inhibited cold active protease, showing it as metalloprotease in nature. The enzyme was sensitive to Cu+2, Zn+2, and Hg+2, and the proteolytic activity decreased upon treatment with heavy metals. The molecular weight of the protease was estimated to be 47 kDa using sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis. Proteins within a specific range of molecular weight possess desirable properties for industrial enzyme use. By working on a specific range, the researchers intended to examine an enzyme to examine its specific characteristics. The purified protease showed high stability to detergents like SDS, Tween 20, Tween 60, and Triton X. The maximum velocity V-max and K-m values were 59.90 mg/min/mL and 1.53 mg/mL, respectively. The obtained protease exhibited an interesting activity at a broad range of pH (6-10) and stability at low temperatures (5-30 & DEG;C) and detergents. Such enzymatic features of versatile and potent cold-active enzymes enhance their industrial applications to meet food, dairy, and laundry requirements.