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Sisymbrium irio Linn is one of the underutilized plants, well-known for its traditional importance in Unani Medicine. The present study aimed to evaluate the antibacterial activities of different polarity-based extracts made from seeds of S.irio (Indian variety). The antibacterial activity of 13 different solvent extracts of S.irio seeds was evaluated by the Agar well-diffusion method. Among 13 different solvent seed extracts, ethanolic extract inhibited the growth of all the three bacterial strains used in the study. Further GC-MS analysis of ethanolic extract was done to reveal its phytochemical constituents. Twenty-five different compounds were identified through GC-MS analysis of ethanolic extract of S.irio seeds. Subsequently, for performing in silico antibacterial studies, the identified phytochemicals were first tested for their drug-likeability through Molinspiration software which yielded four compounds. In silico virtual screening via Autodock Vina was done using four phytochemicals against DNA gyrase subunit B and Dihydrofolate reductase. Out of four phytochemical studied through in silico analysis, "Benzene-1,2-dicarboxylicacid, monoamide, N-(1-cyano-1-methylethyl)" was found to inhibit DNA gyrase subunit B most effectively. The present study revealed that Sisymbrium irio displayed potential antibacterial activity and can be used as a good source for designing potent antibacterial agents. [ABSTRACT FROM AUTHOR]

Background: For centuries, plants have been used in the folk medicine of various cultures for their healing properties. It is amazing how nature has provided us with such powerful remedies. Oxalis corniculata (O. corniculata) has always been used traditionally for its medicinal attributes. In Asia, this herbaceous plant is used for treating many gastrointestinal disorders, such as diarrhea and dysentery. In African folk medicine, on the other hand, this herb is used for respiratory diseases, skin diseases, and fever. Main body: Scientific research has revealed numerous pharmacological potentials of this plant, including antitumor, antimicrobial, antioxidant, anti-inflammatory, and hepatoprotective properties. In addition, studies have indicated that the extract of this plant protects against oxidative stress, inflammation, and various diseases, including cancer and diabetes. Phytochemical analysis of O. corniculata revealed various relevant compounds, including phenolic acids, flavonoids, and alkaloids, which are responsible for its therapeutic properties. Conclusion: The various constituents of this plant have significant ethnomedicinal potential. The plant is a possible source of extracts and chemical compounds with pharmacological activity. In the future, O. corniculata could have an effective role in the development of modern drugs. The objective of this review is to summarize the current knowledge on the medicinal potential of O. corniculata, including its bioactive compounds, mechanisms of action, and therapeutic applications. [ABSTRACT FROM AUTHOR]

Keratinases are proteolytic enzymes that have the capability of degrading insoluble keratin substrates. LS4, LS5, and KS3 were newly isolated strains showing ability to hydrolyze keratins and keratin based products. In this study, different bacterial strains were isolated from soil, screened for protease and keratinase production, and the best isolates were identified. Serial dilution and plating method were used for isolation of pure bacterial culture. Isolated, 48 strains were screened, and their feather degrading ability on feather meal agar plates and keratin azure-based agar. The proteolytic activity of the isolates was also screened on casein agar. Three strains; LS4, LS5, and KS3 shows keratinolytic activity that reveal the keratinase enzyme on medium; feather meal agar, keratin azure agar, and casein agar. Among all the three strains (LS4, LS5, and KS3), KS3 show largest inhibition zone that show maximum enzymatic activity. For its characterization 16S RNA was performed, sequence KS3 was submitted to GenBank and was identified as Bacillus tropicus KS3. Newly isolated strain B. tropicus KS3 showed the keratinase production and highest keratinase activity (35.06 ± 2.5 U/ml). B. tropicus KS3 also show the highest degradation of feather efficiently showed 84% of whole chicken feather biodegradation at 37 °C within 15 days among all the isolated strains. Keratinase enzyme possesses a wide range of potential applications in the bioremediation of feather waste and bio-fertilizer in agricultural land. The industry demands a better source of this enzyme due to its multivariate application and huge market demand. In the present study, a novel keratinase-producing bacteria was isolated and characterized as Bacillus tropicus KS3 from poultry waste contamination soil. [ABSTRACT FROM AUTHOR]

This research article deals with production of industrial enzyme penicillin G acylase from soil bacterial isolates namely AA17A and AA17B, which are selected from 80 soil samples. The strains were selected based on qualitative (turbidity) and quantitative (HPLC) test for 6-aminopenicillanic acid (6APA) production. The enzyme was assayed for its activity and optimized for production of enzyme using design of experiments software (DOE) "Design Expert 8.0.7.1". Optimization of enzyme production of four carbon sources (glucose, glycerol, sucrose and starch), four nitrogen sources (beef extract, tryptone, peptone and yeast extract), for temperature (25°C, 30°C, 35°C and 40°C), four pH (6, 7, 8, 9), four inoculum volumes (2.5 ml, 5.0 ml, 7.5 ml, 10.0 ml) and the phenyl acetic acid (PAA) level (0.15%, 0.17%, 0.185%, 0.2%). The penicillin acylase activity was enhanced to 1.2 fold under following optimized culture conditions: carbon source - glucose (8%), nitrogen source - beef extract (2%), pH 9.0, temperature 30°C, phenyl acetic acid 0.185%, inoculum volume 5 ml. Approximately 1.22-fold purification from the initial culture broth was achieved during ammonium sulphate precipitation (70-80%) with a yield of 4.6% enzyme. The specific activity of the final partially purified enzyme was 13.73 IU/mg protein. [ABSTRACT FROM AUTHOR]