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Extraction and Purification of Extracellular L-Glutamate Oxidase from Streptomyces | ||
| Archives of Razi Institute | ||
| مقالات آماده انتشار، پذیرفته شده، انتشار آنلاین از تاریخ 27 شهریور 1400 اصل مقاله (887.32 K) | ||
| نوع مقاله: Original Articles | ||
| شناسه دیجیتال (DOI): 10.22092/ari.2021.355928.1738 | ||
| نویسندگان | ||
D Hazim Abdul Hameed  ؛ E Hussein Ali
| ||
| Department of Biotechnology – coll, Applied Science, University of Technology, Iraq | ||
| چکیده | ||
| The bacterial isolates Streptomyces were obtained from the soil and cultivated in a wheat bran medium, which is used to produce the L–glutamate oxidase enzyme. The extracellular enzyme was then extracted using a cooling centrifugation process to obtain the filtrate that represents the crude enzyme, after that, the enzyme purification processes were carried out, which included precipitation with ammonium sulfate as a preliminary purification step, followed by dialysis to remove the salts. After that, ion-exchange chromatography and gel filtration were used to finish the purification process, and the enzyme activity was determined for each purification step. The results of purification of L-glutamate oxidase enzyme from streptomyces using ammonium sulfate showed that the specific activity was 8.25 units per milligram protein with a saturation ratio of 60% and the results of purification using dialysis tube showed that the specific activity was 9.5 units per milligram protein and the result of purification using DEAE cellulose ion column showed that the specific activity was 25 unit per milligram protein and the results of purification using gel filtration showed that the specific activity was 56 units per milligram protein which was the best step in purification process due to high enzyme’s specific activity. The optimum temperature and pH for the enzyme’s activity and stability were tested. The results showed that the optimum temperature for the enzyme’s activity was 37 °C and the optimum temperatures for the stability of the enzyme were (30 - 50) °C, while the optimum pH for the activity was 7.0 and the optimum pH for the enzyme stability was (5.0-7.0). | ||
| کلیدواژه‌ها | ||
| L-glutamate oxidase؛ L-glutamate؛ Streptomyces؛ Specific activity | ||
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آمار تعداد مشاهده مقاله: 42 تعداد دریافت فایل اصل مقاله: 12 |
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