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Antimicrobial lectin from Schinus terebinthifolius leaf.

F S Gomes¹, T F Procópio, T H Napoleão

¹Departamento de Bioquímica, CCB, Universidade Federal de Pernambuco, Recife, Brazil.

Journal of Applied Microbiology

|November 30, 2012

Summary

Schinus terebinthifolius leaf lectin (SteLL) was isolated and characterized. This novel lectin demonstrated significant antimicrobial activity against various bacteria and fungi, showing potential for new biomaterial applications.

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Area of Science:

Biochemistry
Microbiology
Natural Products Chemistry

Background:

Schinus terebinthifolius leaves possess traditional medicinal uses against microbial infections.
Lectins are proteins with specific carbohydrate-binding properties, often exhibiting biological activities.

Purpose of the Study:

To isolate and characterize the lectin from Schinus terebinthifolius leaves (SteLL).
To evaluate the antimicrobial activity of the purified SteLL against medically relevant microorganisms.

Main Methods:

Protein extraction from S. terebinthifolius leaves using NaCl.
Purification via activated charcoal filtration and chitin column chromatography.
Characterization of SteLL's properties (molecular weight, stability, inhibition) and determination of antimicrobial activity (MIC, MBC, MFC).

Main Results:

SteLL is a 14-kDa glycopeptide, inhibited by N-acetyl-glucosamine, and stable to heat and pH variations.
Antimicrobial activity was observed against Escherichia coli, Klebsiella pneumoniae, Proteus mirabilis, Pseudomonas aeruginosa, Salmonella enteritidis, and Staphylococcus aureus.
Significant activity was noted against Salmonella enteritidis (MIC: 0.45 μg/mL) and Staphylococcus aureus (MBC: 7.18 μg/mL), as well as Candida albicans (MIC: 6.5 μg/mL, MFC: 26 μg/mL).

Conclusions:

SteLL, a chitin-binding lectin, was successfully purified and exhibits broad-spectrum antimicrobial properties.
This lectin shows promise as a novel biomaterial for developing new antimicrobial agents.