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Antibacterial Activity of Fistulin: A Protease Inhibitor Purified from the Leaves of Cassia fistula

Plant protease inhibitors (PPIs) are one of the important components of a plant's defense machinery. PPIs are active against the insects and microbes which invade the plant. Cassia species possess anti-insecticidal and antimicrobial properties and this study was aimed at investigating the antib...

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Detalles Bibliográficos
Autores principales: Arulpandi, I., Sangeetha, R.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Scholarly Research Network 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3388288/
https://www.ncbi.nlm.nih.gov/pubmed/22779011
http://dx.doi.org/10.5402/2012/584073
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author Arulpandi, I.
Sangeetha, R.
author_facet Arulpandi, I.
Sangeetha, R.
author_sort Arulpandi, I.
collection PubMed
description Plant protease inhibitors (PPIs) are one of the important components of a plant's defense machinery. PPIs are active against the insects and microbes which invade the plant. Cassia species possess anti-insecticidal and antimicrobial properties and this study was aimed at investigating the antibacterial efficacy of a PPI present in the leaves of Cassia fistula. A PPI, fistulin, was isolated from the leaves of C. fistula and purified by gel filtration chromatography. The antibacterial activity of the purified fistulin was studied against five bacterial strains, namely, Bacillus subtilis, Staphylococcus aureus, Klebsiella pneumoniae, Pseudomonas aeruginosa and Escherichia coli. The PPI was found to be very active against S. aureus, E. coli, B. subtilis, and K. pneumonia, and its efficacy was comparable to the standard drug, streptomycin sulphate.
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spelling pubmed-33882882012-07-09 Antibacterial Activity of Fistulin: A Protease Inhibitor Purified from the Leaves of Cassia fistula Arulpandi, I. Sangeetha, R. ISRN Pharm Research Article Plant protease inhibitors (PPIs) are one of the important components of a plant's defense machinery. PPIs are active against the insects and microbes which invade the plant. Cassia species possess anti-insecticidal and antimicrobial properties and this study was aimed at investigating the antibacterial efficacy of a PPI present in the leaves of Cassia fistula. A PPI, fistulin, was isolated from the leaves of C. fistula and purified by gel filtration chromatography. The antibacterial activity of the purified fistulin was studied against five bacterial strains, namely, Bacillus subtilis, Staphylococcus aureus, Klebsiella pneumoniae, Pseudomonas aeruginosa and Escherichia coli. The PPI was found to be very active against S. aureus, E. coli, B. subtilis, and K. pneumonia, and its efficacy was comparable to the standard drug, streptomycin sulphate. International Scholarly Research Network 2012-06-20 /pmc/articles/PMC3388288/ /pubmed/22779011 http://dx.doi.org/10.5402/2012/584073 Text en Copyright © 2012 I. Arulpandi and R. Sangeetha. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Arulpandi, I.
Sangeetha, R.
Antibacterial Activity of Fistulin: A Protease Inhibitor Purified from the Leaves of Cassia fistula
title Antibacterial Activity of Fistulin: A Protease Inhibitor Purified from the Leaves of Cassia fistula
title_full Antibacterial Activity of Fistulin: A Protease Inhibitor Purified from the Leaves of Cassia fistula
title_fullStr Antibacterial Activity of Fistulin: A Protease Inhibitor Purified from the Leaves of Cassia fistula
title_full_unstemmed Antibacterial Activity of Fistulin: A Protease Inhibitor Purified from the Leaves of Cassia fistula
title_short Antibacterial Activity of Fistulin: A Protease Inhibitor Purified from the Leaves of Cassia fistula
title_sort antibacterial activity of fistulin: a protease inhibitor purified from the leaves of cassia fistula
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3388288/
https://www.ncbi.nlm.nih.gov/pubmed/22779011
http://dx.doi.org/10.5402/2012/584073
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