Purification and selected biochemical properties of peroxidase from cress (Lepidium sativum sub sp. sativum)


Altay A., Koktepe T., Durmaz L., Topal F., Gülçin İ., Köksal E.

International Journal of Food Properties, cilt.21, sa.1, ss.2610-2621, 2018 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 21 Sayı: 1
  • Basım Tarihi: 2018
  • Doi Numarası: 10.1080/10942912.2018.1540989
  • Dergi Adı: International Journal of Food Properties
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.2610-2621
  • Anahtar Kelimeler: Cress (Lepidium sativum), peroxidase, enzyme purification, enzyme characterization, enzyme inhabitation, ANHYDRASE ISOENZYMES I, CARBONIC-ANHYDRASE, ANTIOXIDANT ACTIVITY, POLYPHENOL OXIDASE, ENZYME-ACTIVITY, ANTIMICROBIAL ACTIVITIES, AFFINITY-CHROMATOGRAPHY, LACTOPEROXIDASE ENZYME, INHIBITORY PROPERTIES, CRYSTAL-STRUCTURE
  • Erzincan Binali Yıldırım Üniversitesi Adresli: Evet

Özet

© 2018 Ahmet Altaya, Tubanur Koktepea, Lokman Durmaz, Fevzi Topalc, İlhami Gülçin, and Ekrem Köksala. 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.