Pharmacognostical Phytochemical and Biological studies on Euphorbiaceae Family Plant

Abstract

The plant Mallotus philippensis fruits belongs to family Euphorbiaceae which is known as Kamala tree. The following facts justify our interest in this study. The macroscopical, anatomical and powder microscopical studies provides the basis for further identification and authentification of the plant. The outcomes of physicochemical and fluorescence studies on fruits may play a significant role in setting the standards for fruits. Metal analysis from the fruits of Mallotus Philippensis contains mainly mineral elements viz. calcium, chloride, chromium, copper, iron, lead magnesium, manganese, phosphorous, potassium, selenium, sodium and zinc. Preliminary phytochemical screening of total extracts of ethylacetate, ethanolic and aqueous extracts of fruits reveals the presence of flavonoids, alkaloids and terpenoids. TLC, HPLC and HPTLC were performed to support preliminary phytochemical analysis. TLC was performed which gave a positive answer for flavonoids. By HPLC and HPTLC presence of quercetin and rutin was quantified. In-vitro antioxidant study reveals that both the ethanolic and aqueous extracts of Mallotuphilippensis fruits exerts significant free radical scavenging but former is more effective than the later. This antioxidant activity of plant extract maybe due to the presence of flavonoids. The acute toxicological studies showed that the total extract of ethyl acetate, ethanolic and aqueoeus are safe at the dose level of 2000mg/kg b.wt. No sign of mortality was seen in all the extracts of Mallotus Dhilippensis fruits. In Invitro antioxidant studies like DPPH, Nitrousoxide and Hydroxylion methods there was a significant scavenging activity which might due the presence of phenolic compounds such as flavoinoids and tannins. The anti microbial work suggests that plant extracts have significant activity on gram negative bacteria. Molecular docking studies identified for the plant on selective mesenchymal - epithelial transition factor protein kinase has maximum affinity for the protein kinase due to its hydrophobic interaction.