Interaction of plant proteinase inhibitors with gut proteinase of cotton leaf worm, Spodoptera littoralis (Bosid.)
Kholoud Abd Elftah Ibrahim;
Abstract
The present study aimed to investigate the inhibitory effect of partial purified proteinase inhibitor from seeds of soybean Glycine max against the 4th instar larvae of cotton leaf worm Spodoptera littoralis (Bosid.) (Lepidoptera: Noctuidea). This study was divided into two main parts:
The first part of the study was concerned with the purification of proteinase inhibitor from seeds extract of soybean and its inhibitory effect against trypsin and chymotrypsin-like enzyme in midgut extract of 4th larval instar of S. littoralis.
The second part was concerned with the efficiency of purified fractions on serine enzymes activity, larval growth and development after feeding 4th instar larvae on SPI.
1. Purification of proteinase inhibitor and screening of its inhibitory activity.
1.1. Purified fractions of soybean proteinase inhibitor SPI and its inhibitory activity against trypsin-like enzyme from S. littoralis.
Results revealed that, F0-30 (NH4)2SO4 (w/v) saturation was efficient for precipitating the proteinase inhibitor. It gave the highest inhibitory activity against trypsin-like enzyme of 4th instar larvae of S. littoralis; 3.9 ± 0.2 TIU/mg protein. The fold purification obtained from the fraction was 1.56 times that of the crude extract and the recovery percentage was 71.76%.
Followed by F60-90 (NH4)2SO4 which gave 2.7 ± 0.5 TIU/mg protein and F30-60 (NH4)2SO4 showed the lowest trypsin inhibitory activity, 0.5 ± 0.08 TIU/mg protein and lowest fold purification 0.2 times that of crude extract and recovery percentage 12.94%.
1.2. Purified fractions of SPI and its inhibitory activity against chymotrypsin-like enzyme from S. littoralis.
Data indicated that F0-30 (NH4)2SO4 (w/v) saturation was the most effective fraction against chymotrypsin-like enzyme of 4th instar larvae of S. littoralis, it gave the highest inhibitory activity 5.3± 0.2 CIU/mg protein.
Followed by F60-90 (NH4)2SO4 which gave 2.9 ± 0.1 CIU/mg protein with no significant difference with F30-60 (NH4)2SO4 which was 2.7 ± 0.1 CIU/mg protein.
The first part of the study was concerned with the purification of proteinase inhibitor from seeds extract of soybean and its inhibitory effect against trypsin and chymotrypsin-like enzyme in midgut extract of 4th larval instar of S. littoralis.
The second part was concerned with the efficiency of purified fractions on serine enzymes activity, larval growth and development after feeding 4th instar larvae on SPI.
1. Purification of proteinase inhibitor and screening of its inhibitory activity.
1.1. Purified fractions of soybean proteinase inhibitor SPI and its inhibitory activity against trypsin-like enzyme from S. littoralis.
Results revealed that, F0-30 (NH4)2SO4 (w/v) saturation was efficient for precipitating the proteinase inhibitor. It gave the highest inhibitory activity against trypsin-like enzyme of 4th instar larvae of S. littoralis; 3.9 ± 0.2 TIU/mg protein. The fold purification obtained from the fraction was 1.56 times that of the crude extract and the recovery percentage was 71.76%.
Followed by F60-90 (NH4)2SO4 which gave 2.7 ± 0.5 TIU/mg protein and F30-60 (NH4)2SO4 showed the lowest trypsin inhibitory activity, 0.5 ± 0.08 TIU/mg protein and lowest fold purification 0.2 times that of crude extract and recovery percentage 12.94%.
1.2. Purified fractions of SPI and its inhibitory activity against chymotrypsin-like enzyme from S. littoralis.
Data indicated that F0-30 (NH4)2SO4 (w/v) saturation was the most effective fraction against chymotrypsin-like enzyme of 4th instar larvae of S. littoralis, it gave the highest inhibitory activity 5.3± 0.2 CIU/mg protein.
Followed by F60-90 (NH4)2SO4 which gave 2.9 ± 0.1 CIU/mg protein with no significant difference with F30-60 (NH4)2SO4 which was 2.7 ± 0.1 CIU/mg protein.
Other data
| Title | Interaction of plant proteinase inhibitors with gut proteinase of cotton leaf worm, Spodoptera littoralis (Bosid.) | Other Titles | التأثير التفاعلي لمثبطات انزيم البروتينيز النباتية مع انزيمات البروتينيز في معي دودة ورق القطن (رتبة حرشفية الاجنحة) | Authors | Kholoud Abd Elftah Ibrahim | Issue Date | 2021 |
Attached Files
| File | Size | Format | |
|---|---|---|---|
| BB8292.pdf | 696.8 kB | Adobe PDF | View/Open |
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