Mosquitoes are blood-feeding insects and serve as the most important vectors for spreading human diseases such as malaria, yellow fever, dengue fever, and filariasis. The continued use of synthetic insecticides has resulted in resistance in mosquitoes. Synthetic insecticides are toxic and affect the environment by contaminating soil, water, and air, and then natural products may be an alternative to synthetic insecticides because they are effective, biodegradable, eco-friendly, and safe to environment. Botanical origin may serve as suitable alternative biocontrol techniques in the future. Mentha spicata, an edible and medicinal plant, is chiefly distributed in Southeast Asia and South Asia. In the present study, the toxicity of mosquito larvicidal activity of leaf essential oil (EO) and their major chemical constituents from Mentha spicata against Culex quinquefasciatus, Aedes aegypti, and Anopheles stephensi. The chemical composition of the leaf EO was analyzed using gas chromatography-mass spectroscopy (GC-MS). GC-MS revealed that the EO of M. spicata contained 18 compounds. The major chemical components identified were carvone (48.60%), cis-carveol (21.30%), and limonene (11.30%). The EO had a significant toxic effect against early third-stage larvae of C. quinquefasciatus, A. aegypti, and A. stephensi with LC(50) values of 62.62, 56.08, and 49.71 ppm and LC(90) values of 118.70, 110.28, and 100.99 ppm, respectively. The three major pure constituents extracted from the M. spicata leaf EO were also tested individually against three mosquito larvae. The LC(50) values of carvone, cis-carveol, and limonene appeared to be most effective against A. stephensi (LC(50) 19.33, 28.50, and 8.83 ppm) followed by A. aegypti (LC(50) 23.69, 32.88, and 12.01 ppm), and C. quinquefasciatus (LC(50) 25.47, 35.20, and 14.07 ppm). The results could be useful in search for newer, safer, and more effective natural larvicidal agents against C. quinquefasciatus, A. aegypti, and A. stephensi.

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A protease producing marine bacterium, Bacillus halodurans CAS6 isolated from marine sediments, was found to produce higher enzyme by utilizing shrimp shell powder. Optimum culture conditions for protease production were 50 °C, pH 9.0, 30 % NaCl and 1 % shrimp shell powder (SSP) and the protease purified with a specific activity of 509.84 U/mg. The enzyme retained 100 % of its original activity even at 70 °C, pH 10.0 and 30 % NaCl for 1 h. The purified protease exhibited higher stability when treated with ionic, non-ionic (72-94 %) and commercial detergents (76-88 %), and organic solvents (88-126 %). Significant blood stain removal activity was found with the enzyme in washing experiments. The culture supernatant supplemented with 1 % SSP showed 93.67 ± 2.52 % scavenging activity and FT-IR analysis of the reaction mixture confirmed the presence of antioxidants such as cyclohexane and cyclic depsipeptide with aliphatic amino groups. These remarkable qualities found with this enzyme produced by Bacillus halodurans CAS6 could make this as an ideal candidate to develop the industrial process for bioconversion of marine wastes and antioxidant synthesis.