Inhibition of fungal plant pathogens by seed proteins of Harpullia cupanioides (Roxb.)

C. Bharathimatha, Sabitha Doraiswamy, R. Velazhahan

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Seed extracts of 50 plant species belonging to different families were evaluated for their ability to inhibit growth of Trichoderma viride in vitro. Of the various seed extracts, the seed extracts of Harpullia cupanioides (Roxb) belonging to Sapindaceae family exhibited very high antifungal activity. The seed extract of H. cupanioides strongly inhibited the growth of Rhizoctonia solani, Curvularia lunata, Colletotrichum musae and Alternaria alternata. Seed extract of H. cupanioides retained its antifungal activity even after heating at 100°C for 10 min or autoclaving at 121°C for 20 min. For partial purification of antifungal proteins, H. cupanioides seed extract was subjected to ammonium sulphate fractionation followed by gel filtration on Sephadex G-200 column. The fractions from sephadex G-200 were individually tested for their antifungal activity against T. viride. SDS-PAGE analysis of the fractions from Sephadex-G200 column indicated that the fractions with antifungal activity contained a 68-kDa band as well as other low molecular weight protein bands. The N-terminal amino acid sequence of the 68-kDa protein (13 residues) was determined by Edman degradation. However, comparison with sequences in the GenBank database (Swiss Prot) did not reveal any homology with known protein sequences.

Original languageEnglish
Pages (from-to)75-82
Number of pages8
JournalActa Phytopathologica et Entomologica Hungarica
Volume37
Issue number1-3
DOIs
Publication statusPublished - 2002

Fingerprint

seed extracts
plant pathogens
seeds
Trichoderma viride
proteins
amino acid sequences
Colletotrichum musae
antifungal proteins
Sapindaceae
autoclaving
Alternaria alternata
Thanatephorus cucumeris
ammonium sulfate
fractionation
gels
molecular weight
heat
degradation

Keywords

  • Antifungal protein
  • Harpullia cupanioides
  • Trichoderma viride

ASJC Scopus subject areas

  • Plant Science
  • Insect Science

Cite this

Inhibition of fungal plant pathogens by seed proteins of Harpullia cupanioides (Roxb.). / Bharathimatha, C.; Doraiswamy, Sabitha; Velazhahan, R.

In: Acta Phytopathologica et Entomologica Hungarica, Vol. 37, No. 1-3, 2002, p. 75-82.

Research output: Contribution to journalArticle

@article{5599a2715f174bec8fc54f3db7361b82,
title = "Inhibition of fungal plant pathogens by seed proteins of Harpullia cupanioides (Roxb.)",
abstract = "Seed extracts of 50 plant species belonging to different families were evaluated for their ability to inhibit growth of Trichoderma viride in vitro. Of the various seed extracts, the seed extracts of Harpullia cupanioides (Roxb) belonging to Sapindaceae family exhibited very high antifungal activity. The seed extract of H. cupanioides strongly inhibited the growth of Rhizoctonia solani, Curvularia lunata, Colletotrichum musae and Alternaria alternata. Seed extract of H. cupanioides retained its antifungal activity even after heating at 100°C for 10 min or autoclaving at 121°C for 20 min. For partial purification of antifungal proteins, H. cupanioides seed extract was subjected to ammonium sulphate fractionation followed by gel filtration on Sephadex G-200 column. The fractions from sephadex G-200 were individually tested for their antifungal activity against T. viride. SDS-PAGE analysis of the fractions from Sephadex-G200 column indicated that the fractions with antifungal activity contained a 68-kDa band as well as other low molecular weight protein bands. The N-terminal amino acid sequence of the 68-kDa protein (13 residues) was determined by Edman degradation. However, comparison with sequences in the GenBank database (Swiss Prot) did not reveal any homology with known protein sequences.",
keywords = "Antifungal protein, Harpullia cupanioides, Trichoderma viride",
author = "C. Bharathimatha and Sabitha Doraiswamy and R. Velazhahan",
year = "2002",
doi = "10.1556/APhyt.37.2002.1-3.8",
language = "English",
volume = "37",
pages = "75--82",
journal = "Acta Phytopathologica et Entomologica Hungarica",
issn = "0238-1249",
publisher = "Akademiai Kiado",
number = "1-3",

}

TY - JOUR

T1 - Inhibition of fungal plant pathogens by seed proteins of Harpullia cupanioides (Roxb.)

AU - Bharathimatha, C.

AU - Doraiswamy, Sabitha

AU - Velazhahan, R.

PY - 2002

Y1 - 2002

N2 - Seed extracts of 50 plant species belonging to different families were evaluated for their ability to inhibit growth of Trichoderma viride in vitro. Of the various seed extracts, the seed extracts of Harpullia cupanioides (Roxb) belonging to Sapindaceae family exhibited very high antifungal activity. The seed extract of H. cupanioides strongly inhibited the growth of Rhizoctonia solani, Curvularia lunata, Colletotrichum musae and Alternaria alternata. Seed extract of H. cupanioides retained its antifungal activity even after heating at 100°C for 10 min or autoclaving at 121°C for 20 min. For partial purification of antifungal proteins, H. cupanioides seed extract was subjected to ammonium sulphate fractionation followed by gel filtration on Sephadex G-200 column. The fractions from sephadex G-200 were individually tested for their antifungal activity against T. viride. SDS-PAGE analysis of the fractions from Sephadex-G200 column indicated that the fractions with antifungal activity contained a 68-kDa band as well as other low molecular weight protein bands. The N-terminal amino acid sequence of the 68-kDa protein (13 residues) was determined by Edman degradation. However, comparison with sequences in the GenBank database (Swiss Prot) did not reveal any homology with known protein sequences.

AB - Seed extracts of 50 plant species belonging to different families were evaluated for their ability to inhibit growth of Trichoderma viride in vitro. Of the various seed extracts, the seed extracts of Harpullia cupanioides (Roxb) belonging to Sapindaceae family exhibited very high antifungal activity. The seed extract of H. cupanioides strongly inhibited the growth of Rhizoctonia solani, Curvularia lunata, Colletotrichum musae and Alternaria alternata. Seed extract of H. cupanioides retained its antifungal activity even after heating at 100°C for 10 min or autoclaving at 121°C for 20 min. For partial purification of antifungal proteins, H. cupanioides seed extract was subjected to ammonium sulphate fractionation followed by gel filtration on Sephadex G-200 column. The fractions from sephadex G-200 were individually tested for their antifungal activity against T. viride. SDS-PAGE analysis of the fractions from Sephadex-G200 column indicated that the fractions with antifungal activity contained a 68-kDa band as well as other low molecular weight protein bands. The N-terminal amino acid sequence of the 68-kDa protein (13 residues) was determined by Edman degradation. However, comparison with sequences in the GenBank database (Swiss Prot) did not reveal any homology with known protein sequences.

KW - Antifungal protein

KW - Harpullia cupanioides

KW - Trichoderma viride

UR - http://www.scopus.com/inward/record.url?scp=0036347028&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036347028&partnerID=8YFLogxK

U2 - 10.1556/APhyt.37.2002.1-3.8

DO - 10.1556/APhyt.37.2002.1-3.8

M3 - Article

AN - SCOPUS:0036347028

VL - 37

SP - 75

EP - 82

JO - Acta Phytopathologica et Entomologica Hungarica

JF - Acta Phytopathologica et Entomologica Hungarica

SN - 0238-1249

IS - 1-3

ER -