A novel antifungal protein with lysozyme-like activity from seeds of Clitoria ternatea

Appl Biochem Biotechnol. 2014 Jun;173(3):682-93. doi: 10.1007/s12010-014-0880-8. Epub 2014 Apr 2.

Abstract

An antifungal protein with a molecular mass of 14.3 kDa was isolated from the seeds of butterfly pea (Clitoria ternatea) and designated as Ct protein. The antifungal protein was purified using different methods including ammonium sulphate precipitation, ion exchange chromatography on DEAE-cellulose and gel filtration on Sephadex G-50 column. Ct protein formed a single colourless rod-shaped crystal by hanging drop method after 7 days of sample loading. The protein showed lytic activity against Micrococcus luteus and broad-spectrum, fungicidal activity, particularly against the most clinically relevant yeasts, such as Cryptococcus neoformans, Cryptococcus albidus, Cryptococcus laurentii, Candida albicans and Candida parapsilosis. It also exerted an inhibitory activity on mycelial growth in several mould species including Curvularia sp., Alternaria sp., Cladosporium sp., Aspergillus flavus, Aspergillus fumigatus, Aspergillus niger, Rhizopus sp., and Sclerotium sp. The present study adds to the literature on novel seed proteins with antifungal activity.

MeSH terms

  • Antifungal Agents* / chemistry
  • Antifungal Agents* / isolation & purification
  • Antifungal Agents* / pharmacology
  • Clitoria / chemistry*
  • Fungi / growth & development*
  • Muramidase* / chemistry
  • Muramidase* / isolation & purification
  • Muramidase* / pharmacology
  • Plant Proteins* / chemistry
  • Plant Proteins* / isolation & purification
  • Plant Proteins* / pharmacology
  • Seeds / chemistry*

Substances

  • Antifungal Agents
  • Plant Proteins
  • Muramidase