Activity‐guided isolation of a novel protein from Croton tiglium with antifungal and antibacterial activities

Abstract

This study describes the activity-guided isolation and purification of a novel antimicrobial protein from the seed of Croton tiglium Linn. Purification was carried out by (NH(4))(2)SO(4) precipitation, gel filtration and DEAE-cellulose ion-exchange chromatography. Antifungal and antibacterial activities were determined after each purification step. SDS-polyacrylamide gel electrophoresis revealed that the purified protein was a monomer with molecular mass of 50 kDa. This is a first report on purification of a protein from Croton tiglium, which possesses a strong and broad spectrum antimicrobial activity.

In vitro screening of peptidase inhibitory activity in some plants of North India

“…Patriota et al (2016) purified trypsin inhibitor from bignoniaceae family (Tecoma stans) which had an inhibitory effect on growth and promotes ATP depletion and lipid peroxidation in Candida albicans and Candida krusei. Shahid et al (2008) purified a novel protein from Croton tiglium belonging to Euphorbiaceae family with antifungal and antibacterial activities. Similarly, Lone et al (2017) and Chaudhary et al (2008) had purified and characterized trypsin inhibitor from the seeds of Putranjiva roxburghii of Putranjivaceae family by acid precipitation, cation-exchange and anion-exchange chromatography.…”

Antidermatophytic Activity of Ethanolic Extract fromCroton tiglium

“…In a screening of medicinal plants for the antifungal activity, Jamil et al found that crude extracts from the leaves and seeds of C. tiglium were active against Trichocomaceae ( Aspergillus niger and A. tamarii ) and Mucoraceae ( Mucor mucedo and Rhizopus solani ) [ 24 ]. In a separate experiment, Shahid et al discovered that a 50 kDa protein had good antifungal activity [ 18 ]. However, Iraqui and Yadav [ 19 ] have discovered the ethanolic or methanolic extracts from seeds of C. tiglium exhibiting better fungicidal activity against T. rubrum than the water extracts.…”

Activity-Guided Isolation of a Novel Protein From Foeniculum Vulgare With Antifungal and Antibacterial Activities

“…The fraction showing high activity was further purified by ion-exchange chromatography on DEAE-Sephadex A-50 column. The elutions were carried out in a gradient of sodium chloride of different molarity ranging from 0.2-1 M [15]. Molecular mass of the crude protein was determined by SDS-PAGE [16].…”