Potential of ionic liquids for inhibiting the growth and β-lactamase production by Bacillus cereus EMB20.

Present work reports the inhibition of Bacillus cereus EMB20 β-lactamase by a deep eutectic solvent, maline in an uncompetitive manner. Far-UV CD and intrinsic fluorescence spectroscopy revealed a disrupted secondary as well as tertiary structure as a function of maline concentration. The effect of individual components of maline on β-lactamase inhibition showed that malonic acid was mainly responsible for inhibiting the β-lactamase. Structural and docking studies found that malonic acid led to major perturbations in the secondary and tertiary structure of the enzyme while H-bonding with the active site residues. Further the antibacterial and cytotoxic studies also confirmed the potential of maline as a potent growth inhibitor of β-lactamase producing B. cereus EMB20.