Title |
Production of extracellular enzymes in the entomopathogenic fungus Verticillium lecanii
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Authors |
Saba Hasan1*, Anis Ahmad2, Abhinav Purwar1, Nausheen Khan1, Rishi Kundan1 & Garima Gupta1
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Affiliation |
1Amity Institute of Biotechnology, Amity University Uttar Pradesh, Lucknow Campus -226010, India; 2Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh - 202002, India. |
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saba0786@gmail.com; *Corresponding author |
Article Type |
Hypothesis |
Date |
Received January 28, 2013; Accepted January 29, 2013; Published March 02, 2013
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Abstract |
This study investigates the mechanisms as well as strategies for purification and characterization of potential enzymes involved in pathogenesis of entomopathogenic fungi. The test strain of Verticillium lecanii that was screened, during the present investigation, proved to be an efficient producer of protein and polysaccharide degrading enzymes (amylase, protease, and lipase), hence indicating versatility in biochemical mechanisms. Halo zones produced colony growth of V. lecanii on agar confirmed activity of protease, amylase and lipase enzyme by the V. lecanii isolate. Enzymatic Index (EI) observed were: Protease – 2.195, Amylase- 2.196, Lipase- 2.147. Spectrophotometric analysis of enzymatic activity of V.lecanii at five different pH – 3, 5, 7, 9, 11 revealed that highest proteolytic activity of the V. lecanii isolate was reported at pH 7 and 9 whereas proteolytic activity was minimum at acidic pH 3. Maximum amylolytic activity of V. lecanii on the 7th day of inoculation was at pH 3 i.e. in an acidic environment in contrast to neutral pH 7. Maximum lipolytic activity of V. lecanii was found at pH 7. Since enzyme production in entomopathogenic fungi is specific and forms an important criterion for successful development as well as improvement of mycoinsecticides, hence a significant conclusion from the present analysis is the degree of variation in secretion of enzymes in test strain of Verticillium lecanii. |
Keywords |
Verticillium lecanii, Mycoinsecticides, Protease, Amylase, Lipase, Enzymatic Index.
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Citation |
Hasan et al.
Bioinformation 9(5): 238-242 (2013) |
Edited by |
P Kangueane
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ISSN |
0973-2063
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Publisher |
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License |
This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License. |