Purification of catalase from celery (Apium graveolens)
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Abstract (EN)
In this study, catalase enzyme was purified from celery leaves and characterizated. The molecular weight of the purified enzyme was estimated as 236 kDa and the enzyme was consist of four identical subnits with the molecular weight of 59 kDa each. The optimal temperature and pH were found 30°C and 7,5, respectively. Different glycerol solutions were prepared for storage stability of this enzyme and it was incubated in this solutions. The highest storage stability of this enzyme was determined in 20 % glycerol solution. Catalase enzyme showed better thermal stability (28 %) at 25°C than 40°C. Km and Vmax values were 27,5 mM and 87 U/mg protein respectively towards hydrogen peroxide.
Author
Özge Güngör
How to Cite
Özge Güngör (Master Thesis). Purification of catalase from celery (Apium graveolens), 2015, Çukurova University.
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