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http://krishi.icar.gov.in/jspui/handle/123456789/74066
Title: | Extracellular novel metalloprotease from Xenorhabdus indica and its potential as an insecticidal agent. |
Other Titles: | Not Available |
Authors: | Kumar P., Singh, S. Dutta, D., Singh, N. Sharma, G., Ganguly, S., Kalia, V., Nain, L. |
ICAR Data Use Licennce: | http://krishi.icar.gov.in/PDF/ICAR_Data_Use_Licence.pdf |
Author's Affiliated institute: | ICAR::Indian Agricultural Research Institute |
Published/ Complete Date: | 2013-08-09 |
Project Code: | Not Available |
Keywords: | Entomopathogenic nematode, alkaline metalloprotease, Xenorhabdus indica, MALDITOF, Helicoverpa armigera |
Publisher: | The Korean Society for Microbiology and Biotechnology |
Citation: | Not Available10. Kumar P., Singh, S. Dutta, D., Singh, N. Sharma, G., Ganguly, S., Kalia, V., Nain, L. 2013. Extracellular novel metalloprotease from Xenorhabdus indica and its potential as an insecticidal agent. Journal of Microbiology and Biotechnology 23(11): 1536–1543 |
Series/Report no.: | Not Available; |
Abstract/Description: | Proteases produced by Xenorhabdus are known to play a significant role in virulence leading to insect mortality. The present study was undertaken to purify and characterize protease from Xenorhabdus indica, an endosymbiont of nematode Steinernema thermophilum, and to decipher its role in insect mortality and its efficacy to control Helicoverpa armigera. A set of 10 strains of Xenorhabdus isolated from different regions of India were screened for protease activity on the basis of zone of clearing on gelatin agar plates. One potent strain of Xenorhabdus indica was selected for the production of protease, and the highest production (1,552 U/ml) was observed at 15-18 h of incubation at 28oC in soya casein digest broth. The extracellular protease was purified from culture supernatant using ammonium sulfate precipitation and ion-exchange chromatography. The enzyme was further characterized by SDS-PAGE and zymography, which confirmed the purity of the protein and its molecular mass was found to be ~52 kDa. Further MALDI-TOF/TOF analysis and effect of metal chelating agent 1,10-phenanthrolin study revealed the nature of the purified protease as a secreted alkaline metalloprotease. The bioefficacy of the purified protease was also tested against cotton bollworm (Helicoverpa armigera) and resulted in 67.9 ± 0.64% mortality within one week. This purified protease has the potential to be developed as a natural insecticidal agent against a broad range of agriculturally important insects. |
Description: | Not Available |
ISSN: | Not Available |
Type(s) of content: | Research Paper |
Sponsors: | Not Available |
Language: | English |
Name of Journal: | Journal of Microbiology and Biotechnology |
Volume No.: | 23 |
Page Number: | 1536-1543 |
Name of the Division/Regional Station: | Entomology |
Source, DOI or any other URL: | http://dx.doi.org/10.4014/jmb.1306.06062 |
URI: | http://krishi.icar.gov.in/jspui/handle/123456789/74066 |
Appears in Collections: | CS-IARI-Publication |
Files in This Item:
File | Description | Size | Format | |
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JMB023-11-06_FDOC_1.pdf | 1.68 MB | Adobe PDF | View/Open |
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