Editor-in-Chief: Jean-Marc Sabatier Laboratoire ERT 62 'Ingénierie des peptides à visée thérapeutique' Université de la Méditerranée Faculté de Médecine Nord Boulevard Pierre Dramard 13916 - MARSEILLE, Cedex 20 France
Affiliation: Azm Center for Research in Biotechnology and its Applications, Doctoral School of Science and Technology, Lebanese University, El Mittein Street, Tripoli, Lebanon.
The L-amino acid oxidase (LAAO) is a multifunctional enzyme, able to partake in different activities including antibacterial activity. In this study, a novel LAAO (Mb-LAAO) was isolated from the venom of M. bornmuelleri snake using size exclusion chromatography followed by RP-HPLC and partially characterized. However, the molecular weight of the Mb-LAAO determined by ESI-MS and SDS-PAGE was 59 960.4 Da. Once the enzymatic activity test confirming the enzyme’s identity (transformation of L-leucine) was done, the Mb-LAAO was evaluated for its antibacterial activity against Gram-negative bacteria. It showed a remarkable effect against M. morganii and K. pneumoniae. Moreover, no cytotoxic activity was observed for Mb-LAAO against human erythrocytes arguing for an exploration of its pharmaceutical interest.