Abstract
Lysozymes have gained attention for their antiseptic properties. In silico studies have shown that the enzyme containing lysM can act as an antibacterial agent. Binding of the lysM motif of rSELys to peptidoglycan and molecular dynamics simulations showed that the protein-ligand binding is very stable. rSELys (2016 bp) is a new recombinant glycoside hydrolase from the thermophilic bacterium Cohnella sp. A01 (PTCC number: 1921). Protein expression and purification, a single band with an apparent molecular weight of ∼74 kDa was observed by SDS-PAGE. The kinetic parameters were Km 1.163 mg/ml, Vmax 670.3 U/mg, kcat 1675.75 (S−1), and kcat/Km 1440.88 (M−1S−1). Its optimum temperature was 55 °C and pH 8. Temperature stability also showed that the temperature of 50–60 °C retained more than half of its activity after 90 min. Based on the results, rSELys demonstrated antibacterial effects on both Gram-positive and Gram-negative strains, with inhibition zones of 11 and 9 mm, respectively. SEM analysis confirmed hydrolysis activity, the MIC was determined to be 31.25 μg/ml and 3.9 μg/ml, and MBC 0.97 μg/ml, respectively. CD and fluorescence studies showed that up to a temperature of 85 °C and a pH value of 8–12 no structural changes occur, and thermal stability protein was confirmed.
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