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Journal of Environmental Biology

pISSN: 0254-8704 ; eISSN: 2394-0379 ; CODEN: JEBIDP

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    Abstract - Issue Jan 2014, 35 (1)                                     Back


nstantaneous and historical temperature effects on a-pinene

Assessment of anti-insect potential of partially purified pea lectin against melon fruit fly, Bactrocera cucurbitae

 

Amrit Pal Kaur1, Satwinder K. Sohal1*, Manpreet Kaur2 and Jatinder Singh3

1Department of Zoology, Guru Nanak Dev University, Amritsar-143 005, India

2Department of Human Genetics, Guru Nanak Dev University, Amritsar-143 005, India

3Department of Molecular Biology and Biochemistry, Guru Nanak Dev University, Amritsar-143 005, India

*Corresponding Author E-mail: satudhillon@hotmail.com

 

 

 

 Publication Data

Paper received:

25 May 2012

 

Revised received:

08 November 2012

 

Accepted:

24 December 2012

 

Abstract

The partially purified pea lectin from fresh green and dry pea seeds significantly influenced various growth and developmental parameters of melon fruit fly, Bactrocera cucurbitae (Coquillett). The larval period and total development period of the melon fruit fly was prolonged with treatment and a marked inhibitory influence on percentage pupation (p<0.01; p<0.05) and percentage emergence (p<0.01; p<0.05) was noticed. The activity of enzymes was assayed in second instar larvae under the influence of LC50 concentration (42.52ppm) of partially purified lectin from dry seeds at increasing exposure intervals of 24, 48 and 72hr. A significant induction in enzyme activity was observed in acid (p<0.01) and alkaline phosphatases (p<0.01), superoxide dismutase (p<0.05) and catalase (p<0.01), whereas; the activity of esterases was suppressed (p<0.01) with treatment at all exposure intervals. The glutathione S-transferases activity showed a slight variation. The present study clearly showed the anti-insect potential of partially purified pea lectin from dry peas as well as green peas against melon fruit fly and further provides a base for deployment of pea lectin in its purified form for its insecticidal potential.

 

 Key words

Bactrocera cucurbitae, Hydrolases, Oxidoreductases, Pisum sativum agglutinin, Transferases

 

 

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