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Purufication of catalase from the walnut (Juglans regia)

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2015
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Abstract (EN)

In this study, we aimed to purify first time catalase enzyme (E.C.1.11.1.6) from walnut (Juglans regia ), to determine kinetic parameters (Km, Vmax), thermal and storage stabilities of the purified catalase. In the partial purification of catalase enzyme homogenization, ultracentrifugation and PD-10 (Sephadex G-25M) column chromotography steps were used. The optimal pH value of catalase was 8.0 and its optimal temperature was 25°C . Thermal stability of catalase at 25 °C compared to 40 °C and 4 °C in storage stability was higher than 25 °C. Km and Vmax values were 10,4 mM and 159,4 U/mg prot. , respectively. It was determined that the enzyme had 4 equal subunits each weighting 53 kDa and had a total having molecular weight of 212 kDa.

Author

Çağlar Akar

How to Cite

Çağlar Akar (Master Thesis). Purufication of catalase from the walnut (Juglans regia), 2015, Çukurova University.

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