and characterization of a novel thermostable antifungal protein with
chitinase activity from mung bean
Solanki1, S. Kumar1, K. Parihar1, K. Sharma1,
P. Gehlot1*, S.K. Singh2 and R. Pathak2
Microbiology Laboratory, Department of Botany, JNV University, Jodhpur - 342
2Division of Plant
Improvement and Pest Management, Central Arid Zone Research Institute, Jodhpur-342
Author E-mail: email@example.com
Paper received : 23.03.2017
Revised received : 02.08.2017
Accepted : 30.10.2017
proteins are produced by many plant species and participate in defence
mechanisms against number of fungal pathogens. The main objective of the study
was to purify and characterize the thermo-stable antifungal compound with
chitinase activity from mung bean Vigna radiata seeds to assess their
antifungal protein was isolated through ammonium sulphate precipitation
method followed by its purification through ion-exchange chromatography. The
purified protein was characterized by evaluating its antifungal efficacy,
thermal stability, chitinase activity and SDS PAGE profiling.
mass of characterized antifungal protein was 50.6 kDa. Purified protein
exhibited antifungal activity against pathogenic fungi Macrophomina
phaseolina and Magnaporthe grisea and sustained its
thermo-stability up to 60°C with chitinase activity.
isolated antifungal proteins showed unique column chromatographic behaviour,
molecular weight, specificity of chitinase activity and relatively high
thermo-stability with potent antifungal activity. It can be used in different
biomedical and pharmaceutical applications as bio-pesticides.
Characterization of antifungal protein.
© 2018 Triveni Enterprises. All rights reserved. No part of the Journal can
be reproduced in any form without prior permission. Responsibility
regarding the authenticity of the data, and the acceptability of the
conclusions enforced or derived, rest completely with the author(s).