Ekmeklik buğday (Triticum aestivum SSP. Vulgare) bitkisinden peroksidaz enziminin saflaştırılması ve karakterizasyonu

---

Thesis Type: Postgraduate

Institution Of The Thesis: Erzincan Binali Yildirim University, Fen-Edebiyat Fakültesi, Kimya Bölümü, Turkey

Approval Date: 2017

Thesis Language: Turkish

Student: SEVGİ ALTIN

Supervisor: Ekrem Köksal

Open Archive Collection: AVESIS Open Access Collection

Abstract:

The purification and characterization of peroxidase is currently growing of interested since peroxidases have implications in various industrial and biochemical areas. In this study, wheat peroxidase was purified and characterized using different techniques. Peroxidase from wheat was purified using (NH4)2SO4 precipitation, dialysis, CM-Sephadex anion exchange chromatography and SDS-gel electrophoresis. Enzyme kinetics were studied using two substrates: guaiacol and hydrogen peroxide. Km and Vmax values were calculated from Lineweaver-Burk graph for each substrate patterns. Km values for guaiacol and hydrogen peroxide were found as 2,467 and 7,307 respectively. Enzyme activity has been purified 284 folds. The pH and optimum temperature were 5,5 and 40 °C, respectively. Peroxidase had molecular mass of 38,8 kDa as determined by SDS-PAGE. The enzyme was highly inhibited by citric acid and setil trimetil amonyum bromür.