Identification of L-Amino Acid Oxidase (Mb-LAAO) with Antibacterial Activity in the Venom of Montivipera bornmuelleri, a Viper from Lebanon
Mohamad Rima, Claudine Accary, Katia Haddad, Riyad Sadek, Souad Hraoui-Bloquet, Jean C. Desfontis and Ziad Fajloun
Pages 337-343 (7)
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
Antibacterial effect, LAAO activity, L-amino acid oxidase, LC-ESI-MS analysis, Montivipera bornmuelleri.
Azm Center for Research in Biotechnology and its Applications, Doctoral School of Science and Technology, Lebanese University, El Mittein Street, Tripoli, Lebanon.