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Purification, Characterization and Antibacterial Activity of l ‐amino Acid Oxidase from Cerastes cerastes
Author(s) -
HananeFadila ZiadMeziane,
Fatima LarabaDjebari
Publication year - 2014
Publication title -
journal of biochemical and molecular toxicology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.526
H-Index - 58
eISSN - 1099-0461
pISSN - 1095-6670
DOI - 10.1002/jbt.21571
Subject(s) - antibacterial activity , staphylococcus aureus , venom , escherichia coli , microbiology and biotechnology , bacteria , minimum inhibitory concentration , pseudomonas aeruginosa , antibacterial agent , biochemistry , chemistry , biology , antibiotics , genetics , gene
Antibiotic resistance presents a real problem in which new antibacterial molecules from natural secretions could be beneficial in the development of new drugs. In this study, Cerastes cerastes venom was investigated for its antibacterial activity against Gram‐positive and Gram‐negative bacteria. The antibacterial activity was evaluated by measuring the halo inhibition and minimum inhibitory concentration (MIC). An l ‐amino acid oxidase (CcLAAO) was purified from this venom using three chromatographic steps; its homogeneity (60 kDa) was confirmed by SDS‐PAGE. LC–MS/MS analysis of CcLAAO showed similarities with other LAAO enzymes from Echis ocellatus and Viridovipera stejnegeri venoms. CcLAAO presents an antibacterial activity against three bacterial strains ( Staphylococcus aureus , Methicillin‐resistant S. aureus , and Pseudomonas aeruginosa ) with MIC values of 10, 10, and 20 μg/mL, respectively. However, no effect was observed against Escherichia coli and yeast strains. Kinetic parameters of CcLAAO evaluated on l ‐leucine at pH 8.0 and 20°C were K m = 0.06 mmol and V max = 164 mmol/min.