Chemical investigation of the methanolic extract of pomegranate fruit following antibacterial activity directed isolation led to the isolation of pelargonidin-3-galactose, cyanidin-3-glucose, gallic acid, quercetin, and myricetin. All these compounds exhibited substantial activity against species of corynebacteria, staphylococci, streptococci, Bacillus subtilis, Shigella, Salmonella, Vibrio cholera, and Escherichia coli. However, all these compounds were more active against Gram-positive species. On comparing the activity of all the isolated pure compounds, it was found that gallic acid showed the highest antibacterial activity against all the tested sensitive strains and the activity of the remaining pure compounds was almost same due to the structural similarities of the compounds. The reason for antibacterial activity of all pure compounds was attributed to their phenolic structure.

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The chemical investigation of the ethanolic extract of the root bark of Onosma hispidum following antibacterial activity directed isolation led to the isolation of 4-hydroxy-3-methoxy cinnamic acid (ferulic acid) and 4-hydroxy-3-methoxy benzoic acid (vanillic acid) which have been reported for the first time in this species. In addition to these compounds, the crude ethanolic extract and methanol fraction exhibited substantial bioactivity against species of corynebacteria, enterococci, staphylococci and streptococci. Ferulic acid was found more bioactive (being relatively more hydrophobic) compared to vanillic acid.

Lactase phlorizin hydrolase is a small intestinal brush border enzyme that catalyzes the hydrolysis of the milk sugar, lactose, and also many flavonoid glucosides. We demonstrate that epigallocatechin-3-gallate (EGCG), the principal flavonoid from green tea, inhibits in vitro hydrolysis of lactose by intestinal lactase. We then tested the hypothesis that salivary proline-rich proteins (PRPs) could modulate this inhibition and stabilize EGCG. Inhibition by EGCG of digestive enzymes (α-amylase>chymotrypsin>trypsin>lactase≫pepsin) was alleviated ∼2-6-fold by PRPs. Furthermore, PRPs appeared stable to proteolysis and also stabilized EGCG under digestive conditions in vitro. This is the first report on EGCG inhibition of lactase, and it quantifies the protective role of PRPs against EGCG inhibition of digestive enzymes.