Madras Agricultural Journal
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Research Article | Open Access | Peer Review

Determination of Detoxifying Enzyme Activity of Gut Isolates of Diamondback Moth, Plutella xylostella (Lepidoptera: Plutellidae) and Effect of Antibiotics on Host Insect Morphogenesis

Indiragandhi P Anandham R Tongmin Sa
Volume : 109
Issue: September(7-9)
Pages: 56 - 62
Downloads: 0
Published: June 20, 2022
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Abstract


Microorganisms present in the host insect gut contributes to nutrient digestion, detoxification, and degradation of toxic substances and produce biologically active metabolites. Gut bacterial strains isolated from Plutella xylostella were tested for their glutathione-S-transferase (GST) and protease activity. The GST activity varied with different bacterial strains and the maximum was recorded for Stenotrophomonas sp. PRGB08 (140 µmoL min-1 mg protein-1) isolated from resistant population. Irrespective to the origin, the substrate preference of the GST enzymes suggested that bacterially derived enzymes contribute for the detoxification of toxic substances and may confer resistance development. N-acyl homoserine lactone produced by the gut bacterial strain Stenotrophomonas sp. PRGB08 suggested that the contribution of gut bacteria to the host insect process might be variable. Furthermore, the experimental elimination of gut bacterial strains resulted in the emergence of malformed adults and adults with less fecundity. This revealed the potential for the new management strategy against the devastating, resistance developed insect species.

DOI
Pages
56 - 62
Creative Commons
Copyright
© The Author(s), 2025. Published by Madras Agricultural Students' Union in Madras Agricultural Journal (MAJ). This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium, provided the original work is properly cited by the user.

Keywords


Insect gut microbe; glutathion-S-transferase; protease; N-acyl homoserine lactone; host biology
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