Purification of a lectin from Eugenia uniflora L. seeds and its potential antibacterial activity
M D L Oliveira1, C A S Andrade, N S Santos-Magalhães
1Departamento de Bioquímica - Laboratório de Glicoproteínas, Universidade Federal de Pernambuco, Recife, PE, Brazil.
Aims:
The aim of this work was to analyse the antimicrobial properties of a purified lectin from Eugenia uniflora L. seeds.
Methods And Results:
The E. uniflora lectin (EuniSL) was isolated from the seed extract and purified by ion-exchange chromatography in DEAE-Sephadex with a purification factor of 11.68. The purified lectin showed a single band on denaturing electrophoresis, with a molecular mass of 67 kDa. EuniSL agglutinated rabbit and human erythrocytes with a higher specificity for rabbit erythrocytes. The haemagglutination was not inhibited by the tested carbohydrates but glycoproteins exerted a strong inhibitory action. The lectin proved to be thermo resistant with the highest stability at pH 6.5 and divalent ions did not affect its activity. EuniSL demonstrated a remarkable nonselective antibacterial activity. EuniSL strongly inhibited the growth of Staphylococcus aureus, Pseudomonas aeruginosa and Klebsiella sp. with a minimum inhibitory concentration (MIC) of 1.5 microg ml(-1), and moderately inhibited the growth of Bacillus subtilis, Streptococcus sp. and Escherichia coli with a MIC of 16.5 microg ml(-1).
Conclusions:
EuniSL was found to be effective against bacteria.
Significance And Impact Of The Study:
The strong antibacterial activity of the studied lectin indicates a high potential for clinical microbiology and therapeutic applications.
