RESUMEN

The study aimed to investigate the antibacterial activity of Mustard (Brassica juncea) and Moringa (Moringa oleifera) leaf extracts and coagulant protein for their potential application in water treatment. Bacterial cell aggregation and growth kinetics studies were employed for thirteen bacterial strains with different concentrations of leaf extracts and coagulant protein. Moringa oleifera leaf extract (MOS) and coagulant protein showed cell aggregation against ten bacterial strains, whereas leaf extract alone showed growth inhibition of five bacterial strains for up to 6 h and five bacterial strains for up to 3 h. Brassica juncea leaf extract (BJS) showed growth inhibition for up to 6 h, and three bacterial strains showed inhibition for up to 3 h. The highest inhibition concentration with 2.5 mg/mL was 19 mm, and furthermore, the minimum inhibitory concentration (MIC) (0.5 mg/mL) and MBC (1.5 mg/mL) were determined to have a higher antibacterial effect for <3 KDa peptides. Based on LCMS analysis, napin was identified in both MOS and BJS; furthermore, the mode of action of napin peptide was determined on lipoprotein X complex (LpxC) and four-chained structured binding protein of bacterial type II topoisomerase (4PLB). The docking analysis has exhibited moderate to potent inhibition with a range of dock score -912.9 Kcal/mol. Thus, it possesses antibacterial-coagulant potential bioactive peptides present in the Moringa oleifera purified protein (MOP) and Brassica juncea purified protein (BJP) that could act as an effective antimicrobial agent to replace currently available antibiotics. The result implies that MOP and Brassica juncea purified coagulant (BJP) proteins may perform a wide degree of antibacterial functions against different pathogens.

Asunto(s)

Albuminas 2S de Plantas/química , Antibacterianos/química , Bacterias Gramnegativas/efectos de los fármacos , Bacterias Grampositivas/efectos de los fármacos , Moringa oleifera/química , Planta de la Mostaza/química , Albuminas 2S de Plantas/aislamiento & purificación , Albuminas 2S de Plantas/farmacología , Amidohidrolasas/antagonistas & inhibidores , Amidohidrolasas/química , Amidohidrolasas/genética , Amidohidrolasas/metabolismo , Antibacterianos/aislamiento & purificación , Antibacterianos/farmacología , Sitios de Unión , ADN-Topoisomerasas de Tipo II/química , ADN-Topoisomerasas de Tipo II/genética , ADN-Topoisomerasas de Tipo II/metabolismo , Bacterias Gramnegativas/enzimología , Bacterias Gramnegativas/crecimiento & desarrollo , Bacterias Grampositivas/enzimología , Bacterias Grampositivas/crecimiento & desarrollo , Pruebas de Sensibilidad Microbiana , Simulación del Acoplamiento Molecular , Extractos Vegetales/química , Hojas de la Planta/química , Unión Proteica , Conformación Proteica en Hélice alfa , Conformación Proteica en Lámina beta , Dominios y Motivos de Interacción de Proteínas

RESUMEN

The aim of the study was to investigate the antibacterial and anticoagulant activity of Moringa (Moringa oleifera) seed extracts and coagulant protein for their potential application in water treatment. Pathogenic microorganisms were obtained from Ramachandra Hospital, Chennai, India. Bacterial cell aggregation and growth kinetics studies were employed for six bacterial strains with different concentrations of seed extracts and coagulant protein. Moringa seed extract and coagulant protein showed cell aggregation against six bacterial strains, whereas seed extract alone showed growth inhibition of all six bacterial strains for up to 6 h, compared to that of control. Escherichia coli and Salmonella para typhi B did not develop resistance against coagulant protein. The results imply that Moringa oleifera is likely an efficient low-molecular bioactive peptide (with <7.5 kDa plant-based coagulant and antimicrobial peptides, confirmed by applying amino acid sequences), using liquid chromatography-mass spectrometry and HPLC, with the corresponding sequences from Napin-1A peptide posing different degrees of antibacterial activity against different pathogenic organisms.