Phospholipases are one of the principal toxic components of snake venom inducing a wide variety of pharmacological activities after envenomation.Natural inhibitors are known to inhibit toxic effects of snake venom enzymes. In this study, ethanol crude extract of M. oleifera was partitioned using n-hexane and ethyl acetateafter which fractionation was done using column and thin layer chromatography. Subsequently,the inhibitory activities of the crude extract and sub-fractions of M. oleifera were investigated against phospholipase enzymes isolated from Naja haje and Naja nigricollis venoms in vitroandin-silicowhile EchiTab-PLUSpolyvalent antivenom was used as the standard drug. The molecular weight of isolated N. Haje phospholipase (NH-PL) and N. nigricollisphospholipase (NN-PL)were24.11 and 35.22 kDa respectively while NH-PL enzymes had specific activity of 2.70 μM/min/mg substrate, NN-PL activity was 2.10μM/min/mgsubstrate.Furthermore, Kmof NH-PL was 0.330 μM with Vmaxof 0.085 μM/mL.min while NN-PL had Vmaxof 0.198 μM/mL.minand Km of 0.670 μM.M. oleiferan-hexane sub-fraction 5 (MOLH5)displayed a complete inhibition of NN-PL enzyme athigh concentrations and achieved total inhibition against NH-PL enzyme activity at all concentrations used. Molecular docking of the phytoconstituents of n-hexane sub-fraction(MOLH5) against venom phospholipase A2 showed 2-Hydrazino-8-hydroxy-4-phenylquinoline, the lead with a docking of -6.789 kcal/mol. Further in-silico studies revealed the lead as a potential drug candidate.Results indicated that the presence of natural inhibitors of phospholipases in M. oleiferan-hexane sub-fraction could assist in the development of alternative therapy in the treatment of snake envenoming.