الفهرس 
IntroductionOnly 14 pages are availabe for public view
 |  | from | 32 |  |  |
| | | from | 32 | | |
Abstract
This research aimed to purify glucose isomerase from Bacillus thurinigenisis and studying its characteristics as well as its immobilization. The results revealed the following points. Glucose isomerase was purified to 42.8 units mg-1 with 15.8 - fold using 80% ammonium sulphate and sephadex G-150. The optimal pH and optimal temperature were 7.0 and 50°C.The optimal glucose concentration for maximum catalytic activity was 8 mM. Ascorbic acid (vitamin c) and folic acid activated glucose isomerase at both 1mM and 2mM. Mn2+ and Ca2+ were the most activating cations for the purified glucose isomerase, however Cd2+, Zn2+ and Co2+ were inhibitors. Ca2+ was the best activator. Sodium sulphate was activator for glucose isomerase whereas sodium bromide, sodium fluoride, sodium azide and sodium arsenate were inhibitors.