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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]

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]

The discovery of antibiotics initiated the era of drug innovation and implementation for human and animal health. Very soon, antibiotic resistance started evolving due to over-prescription and heavy usage of drugs leading to deleterious side effects. However, using plant extracts or medicinal plants has emerged as a new approach to dealing with the current problem. One such medicinal plant Sisymbrium irio L. is widely used in Unani therapy as an antimicrobial, analgesic, antipyretic, antioxidant, anti-inflammatory, hepatoprotective, bronchoprotective etc. The phytochemicals extracted from the aerial part of the plant have been used as a natural compound library and screened against a well-known anti-bacterial drug target Dihydrofolate reductase (DHFR) enzyme of Staphylococcus aureus. The top two phytochemicals with lower docking score along with the positive control were subjected to molecular dynamics (MD) simulation studies to examine the stabilities of the complexes over 100 ns, followed by binding free energy estimation. The Root Mean Square Deviation (RMSD), Root Mean Square Fluctuation (RMSF) and Radius of Gyration (Rg) yielded established results throughout the MD run. Moreover, the derived phytochemicals exhibited lower binding free energy values than the positive control that can be tested for its in vitro efficacy, followed by further optimization to attain a potent therapeutic against S. aureus. Taken together, the present study suggests two promising phytochemicals derived from the aerial part of the plant S. irio with stable MD simulation results, strong binding affinity and no side effects. [ABSTRACT FROM AUTHOR]

Sisymbrium irio Linn belonging to family 'Cruciferae' is one of the well-known plant used in Unani Thearpy. Several studies done throughout the world on 'Sisymbrium irio L', also known as 'London Rocket' or 'Khakshi' has established that this annual herb is of tremendous medicinal benefits. This plant exhibits potential pharmacological activities such as antimicrobial, antioxidant, anti-inflammatory, analgesic, antipyretic, anticancer, detoxify spleen and liver, also used as febrifuge, expectorant, diuretic and used in the treatment of rheumatoid, voice disorders, boils, pimples, cough, and has bronchoprotective and hepatoprotective role. Various phytochemicals have been isolated scientifically from the different parts of the plants such as flavonoids, alkaloids, tannins, saponins, terpinoids, carbohydrates, phenolics compounds, fatty acids, steroids, amino acids and proteins which were found to be of 'Chemotherapeutic Interest'. This review paper summarizes the botanical description, ethnomedical, phytochemical and therapeutical role of the plant and highlighted the need of future research on this plant as a source of novel drug. [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]

Abstract: Triosephosphate isomerase (TIM) is a major enzyme in the glycolytic pathway, which catalyzes the interconversion of glyceraldehyde 3-phosphate to dihydroxyacetone phosphate. Here, we report cloning, expression and purification of a catalytically active recombinant TIM of Leishmania donovani (LdTIM). The recombinant LdTIM had a pH optimum in the range of 7.2–9.0, found stable at 25°C for 30min and K m and V max for the substrate glyceraldehyde 3-phosphate was 0.328±0.02mM and 10.05mM/min/mg, respectively. The cysteine-reactive agent methylmethane thiosulphonate (MMTS) was used as probe, in order to test its effect on enzyme activity. The MMTS induced 75% enzyme inactivation within 15min at 250μM concentration. The biochemical characterization of LdTIM described in this work is the essential step towards deeper understanding of its role in parasite survival. The purification of LdTIM in bioactive form provides important tools for further functional and structural studies. [Copyright &y& Elsevier]

Squalene synthase (SSN, EC 2.5.1.21), a major enzyme in the sterol biosynthetic pathway, catalyses an unusual head-to-head reductive dimerization of two molecules of farnesyl-pyrophosphate (FPP) in a two-step reaction to form squalene. FPP serves as a metabolic intermediate in the formation of sterols, dolichols, ubiquinones and farnesylated proteins. Here, we report cloning, expression and purification of a catalytically active recombinant squalene synthase of Leishmania donovani ( LdSSN). The pH and temperature optima of LdSSN were 7.4 and 37 °C, respectively. Biochemical studies revealed that the Km and Vmax for the substrate FPP were 3.8 μM and 0.59 nM min−1 mg−1 and for NADPH were 43.23 μM and 0.56 nM min−1 mg−1. LdSSN was found to be sensitive towards denaturants as manifested by a loss of enzyme activity at the concentration of 1 M urea or 0.25 M guanidine hydrochloride. Zaragozic acid A, a potent inhibitor of mammalian SSN, was also a competitive inhibitor of recombinant LdSSN, with a Ki of 74 nM. This is the first report on the purification and characterization of full-length recombinant SSN from L. donovani. Studies on recombinant LdSSN will help in evaluating this enzyme as a potential drug target for visceral leishmaniasis. [ABSTRACT FROM AUTHOR]

Enzymes are the biocatalysts synthesized by living organisms having high specificity, catalytic activity, and a broad range of applicability. One such biotechnologically relevant enzyme is keratinase with various industrial applications that capture a significant place in the enzyme market. It belongs to the proteolytic enzyme group that cleaves the highly stable and fibrous protein, keratin through hydrolysis. Keratins are hard-degrading fibrous proteins insoluble in natural solvents and water. It is frequently aggregated in nature and expressively present in the plumes, hair, nail, horn, skins, feet, etc. The broad range of microorganisms, such as bacteria, fungi, and actinomycetes, have been accounted for producing keratinases with significant biotechnological applications. Successful application of this group of enzymes has been seen in various industries such as farming, laundry detergent, cosmetics, animal feed, pharmaceutical, leather, and textile. Moreover, they have found remarkable usability in environment friendly waste management also. This paper focuses on the structure, sources, and various applications of this industrially important enzyme., (Copyright© Bentham Science Publishers; For any queries, please email at epub@benthamscience.net.)

Leptospirosis is considered as one of the most neglected zoonotic tropical diseases. Animals and humans acquire this infection through direct contact with contaminated urine or body fluids of infected animals. This prospective study was undertaken to know the proportion of leptospirosis in pediatric patients presented with acute febrile illness at the Post Graduate Department of Microbiology, King George's Medical University, Lucknow, Uttar Pradesh. Blood samples were collected over a period of one year from January to December 2018 from 70 pediatric patients aged up to 0-12 years presented with febrile illness for 3-14 days. Out of the 70 samples, 7 (10%) samples were found positive by IgM ELISA, 4 (5.7%) samples were positive by MAT and 3(4.3%) were found positive by PCR. Risk factors such as contact with infected animals and contaminated environment were highly associated with seropositivity of leptospirosis. Clinical symptoms such as fever, chills, myalgia, headache, abdominal pain and cough were significantly associated (p < 0.05) with the seropositivity of leptospirosis., Competing Interests: Declaration of competing interest The authors declare that they have no competing interests., (Copyright © 2021 Indian Association of Medical Microbiologists. Published by Elsevier B.V. All rights reserved.)