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- MakaleAçık Erişim2018Scopus SJRQ2Purification and selected biochemical properties of peroxidase from cress (Lepidium sativum sub sp. sativum)
Altay, Ahmet; Koktepe, Tubanur; Durmaz, Lokman; Topal, Fevzi; Gülçin, İlhami; Köksal, Ekrem
Cress (Lepidium sativum) is an annual herb from Brassicaceae family, and in some regions. It is known as peppergrass, garden cress, garden pepper-cress, pepperwort, or poor man’s pepper. Cress is an important medicinal plant in some countries including Turkey. This plant has major scientific and therapeutic significance. Peroxidase (POD, E.C.1.11.1.7) is an oxidor-eductase enzyme produced by a number of organisms. In this study, POD enzyme was purified from cress by ammonium sulphate precipitation, gel filtration, and CM-Sephadex ion-exchange chromatographies. K m and V max values were calculated from the Lineweaver-Burk graph for H 2 O 2 and guaiacol substrates and the substrate specificity of POD was investigated. The results showed that substrate specificity of H 2 O 2 is better than substrate specificity of guaiacol for this enzyme. The inhibition effects of three cations (Al 3+ , Cu 2+ , and Cr 3+ ) and one organic compound of cetyl trimethylammonium bromide were performed and their inhibition types were determined. Finally, optimum pH, optimum temperature, optimum ionic strength, and stable pH were determined.
AtıfScopus14WoS15İncele
- MakaleYalnız künye2013Scopus SJRQ3Changes in chemical composition and peroxidase activity of turnip (Brassica rapa) during processing and frozen storage
Okcu, Zühal; Keleş, Fevzi; Şat, Ihsan Güngör
Chemical composition content and peroxidase enzyme activity of raw, canned and frozen turnip roots were determined. The peroxidase activity determined in the roots of raw turnip was 134x105 EU/100 g fresh weight and 170x105 EU/g protein. There were significant changes in the activities of peroxidase of canned and frozen turnip roots, as well as in the contents of protein. The peroxidase activity of canned turnip roots was practically undetectable while there was residual activity after blanching and freezing. Peroxidase is one of the most heat-stable enzymes in plants. This study shows that heat treatment of 3 min at 95°C is preferred for POD activity inactivating compared with other heat treatment. In addition, conserving process inactivated of POD activity, too.
AtıfScopus3WoS2İncele
