This study characterized cellulase and -Amylase from the plant-parasitic nematode Ditylenchus destructor using integrated computational and experimental approaches to identify reliable industrial biocatalysts. Wet-lab validation via Bradford assay, DNS assay, and Filter Paper Assay (FPA) confirmed enzyme presence and catalytic activity. Molecular docking yielded strong Glide XP scores, indicating high substrate affinity for cellulose and starch. Subsequent 100 ns explicit-solvent MD simulations confirmed remarkable dynamic stability, evidenced by consistently low C-RMSD values (4.0–4.8 Å) and stable radius of gyration profiles (3.68–3.84 nm). Persistent hydrogen bonds and hydrophobic contacts with key active-site residues GLN-131 and ASN-98 in cellulase, GLU-274 and HIS-242 in -Amylase underpin complex stability. These findings collectively position D. destructor enzymes as promising next-generation industrial biocatalyst candidates for food processing and biofuel applications. However, further biochemical validation and empirical kinetic testing under industrially relevant conditions remain necessary to confirm scalability, while the identified residues provide a molecular blueprint for future enzyme engineering initiatives.
Chauhan Hitesh, Prajapati Amarshi, Mohsin Ali et al.· Indian Journal of Nematology· 0 citations
Antimicrobial resistance (AMR) continues to challenge global healthcare by reducing the effectiveness of existing antibacterial therapies. Resistant organisms such as methicillin-resistant Staphylococcus aureus (MRSA) and vancomycin-resistant Enterococcus (VRE) pose significant therapeutic challenges, underscoring the need for new antimicrobial candidates with improved antibacterial potential. The present study aimed to design, synthesize, characterize, and biologically evaluate a series of novel imidazole-thiol conjugates containing aminopyridine, chlorinated aromatic, nitroaromatic, and heteroaromatic moieties. The chemical structures of the synthesized compounds were characterized using FTIR, 1H NMR, 13C NMR, and mass spectrometry. The synthesized derivatives exhibited antibacterial activity against both Gram-positive and Gram-negative bacteria, including resistant strains such as MRSA and VRE. Among the synthesized derivatives, BS2 and BS3 exhibited the lowest minimum inhibitory concentration (MIC) values against the tested resistant strains. Computational studies, including molecular docking against Staphylococcus aureus enoyl-acyl carrier protein reductase (SaFabI; PDB ID: 4ALL), molecular dynamics (MD) simulations, and MM/GBSA analyses, supported the predicted interaction of BS3 with the active site of SaFabI under the simulated conditions. In addition, BS3 exhibited moderate antioxidant activity, protected plasmid DNA against oxidative damage in the Fenton reagent-mediated DNA nicking assay, and demonstrated concentration-dependent cytotoxicity with acceptable cell viability at lower concentrations. In silico ADMET and toxicity analyses indicated acceptable drug-like and toxicity characteristics. Overall, BS3 was identified as a potential lead compound for further optimization as an antimicrobial agent.
Bhargav Devliya, Bimalkumar Patel, Shreya J. Chauhan et al.· Bioorganic chemistry (Print)· 1 citation
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