Show/Hide Menu
Hide/Show Apps
anonymousUser
Logout
Türkçe
Türkçe
Search
Search
Login
Login
OpenMETU
OpenMETU
About
About
Open Science Policy
Open Science Policy
Frequently Asked Questions
Frequently Asked Questions
Communities & Collections
Communities & Collections
Identification and characterization of hydrolytic enzymes from the midgut of the cotton bollworm, Helicoverpa armigera Hubner (Lepidoptera: Noctuidae)
Date
2009-01-01
Author
Ozgur, Ebru
Yucel, Meral
Öktem, Hüseyin Avni
Metadata
Show full item record
This work is licensed under a
Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License
.
Item Usage Stats
1
views
0
downloads
Midgut hydrolytic enzymes of Helicoverpa armigera Hubner (Lepidoptera: Noctuidae) were identified and partially characterized. K-m, V-max, optimum pH, and specific activity were determined for proteolytic enzymes and alpha-amylases. All hydrolytic enzyme activity had an optimum pH value in the alkaline pH range. We observed major serine protease activity, together with minor cysteine-like activity, the former being significantly inhibited by soybean trypsin inhibitor (SBTI) and aprotinin. Moreover, different degrees of inhibition were observed with synthetic protease inhibitors. Electrophoretic methods revealed 3 isozymes of alpha-amylases, of which 2 had higher molecular weight and were more active than the other. Inhibition of amylolytic activity was observed with wheat alpha-amylase inhibitor (WAAI), whereas partially purified maize, chickpea, and bean seed crude extracts did not exhibit inhibitory activity toward alpha-amylases. To the best of our knowledge this is the first report on the properties of alpha-amylases from Helicoverpa armigera and the effects of several plant-originated alpha-amylase inhibitors on them.
Subject Keywords
Helicoverpa armigera
,
Protease
,
Protease inhibitors
,
Alpha-amylase
,
Alpha-amylase inhibitors
URI
https://hdl.handle.net/11511/39226
Journal
TURKISH JOURNAL OF AGRICULTURE AND FORESTRY
DOI
https://doi.org/10.3906/tar-0802-5
Collections
Department of Biology, Article