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Abstract - Issue Nov 2015, 36 (6) Back
nstantaneous and historical temperature effects on a-pinene
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Assessment
of Sauromatum guttatum lectin toxicity against Bactrocera
cucurbitae
Manpreet Kaur1,
Kshema Thakur2, Sukhdev Singh Kamboj2, Satwinder Kaur3,
Amritpal Kaur3 and Jatinder Singh2*
1Department of
Human Genetics, Guru Nanak Dev University, Amritsar-143 005, India
2Department of
Molecular Biology and Biochemistry, Guru Nanak Dev University, Amritsar-143
005, India
3Department of
Zoology, Guru Nanak Dev University, Amritsar-143 005, India
* Corresponding Author?s
Email : jatinderarora2009@gmail.com
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Publication
Data
Paper received:
29 July 2014
Revised received:
23 January 2015
Accepted:
20 March 2015
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Abstract
Lectins
are proteins that bind specifically to foreign glycans. Due to this binding
property, these molecules have potential application as bioinsecticidal tools
replacing conventional chemical insecticides. The present study involved
purification of phytolectin from the tubers of Sauromatum guttatum by
affinity chromatography on asialofetuin-linked silica matrix. The purity of
the sample was checked by SDS-PAGE at pH 8.3. Purified lectin was
incorporated in the artificial diet of a Dipteran model, Bactrocera
cucurbitae at different concentrations (10, 20, 40, 60 and 80 μgml-1).
The lectin significantly affected various developmental parameters that were
studied. Percentage pupation and percentage emergence was reduced to 44 % and
7.9%, respectively, at 80 μgml-1 concentration as compared to
control (100 %). LC50 of Sauromatum guttatum lectin was
calculated to be 19.42 μgml-1. Treatment of insect larvae
with LC50 of Sauromatum guttatum lectin suppressed the
activity of hydrolytic enzymes (esterases and acid phosphatases) and
oxidative enzymes (superoxide dismutase and glutathione-S-transferase). Thus,
with low LC50 and high mortality (approximately 92 % at 80
μgml-1) of the insect larvae, Sauromatum guttatum
lectin offers a possibility to engineer crop plants for improved and safer
agriculture.
Key
words
Anti-oxidative
enzymes, Araceae, Artificial diet bioassay, Hydrolytic enzymes, Tephritidae
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enforced or derived, rest completely with the author(s).
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