Purification of peroxidase from Amsonia orientalis by three-phase partitioning and its biochemical characterization
SEPARATION SCIENCE AND TECHNOLOGY, cilt.53, sa.5, ss.756-766, 2018 (SCI-Expanded, Scopus)
- Yayın Türü: Makale / Tam Makale
- Cilt numarası: 53 Sayı: 5
- Basım Tarihi: 2018
- Doi Numarası: 10.1080/01496395.2017.1405990
- Dergi Adı: SEPARATION SCIENCE AND TECHNOLOGY
- Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
- Sayfa Sayıları: ss.756-766
- Anahtar Kelimeler: Activity recovery, molecular weight, peroxidase, purification, three-phase partitioning, CABBAGE BRASSICA-OLERACEA, TUBERS SOLANUM-TUBEROSUM, III PLANT PEROXIDASES, CRYSTAL-STRUCTURE, EFFICIENT METHOD, VAR.-CAPITATA, PROTEINS, RECOVERY, ENZYME, L.
- Kocaeli Üniversitesi Adresli: Evet
Özet
The present work describes the purification and characterization of peroxidase from the medicinal plant, Amsonia orientalis, for the first time. The activity recovery for peroxidase was 162% with 12.5-fold purification. Optimal purification parameters were 20% (w/v) (NH4)(2)SO4 saturation at pH 6.0 and 25 degrees C with 1.0:1.0 (v/v) ratio of crude extract to t-butanol ratio for 30 min. The molecular mass of the enzyme was found to be ca. 59 kDa. Peroxidase showed K-m values of 1.88 and 2.0 mM for pyrogallol and hydrogen peroxide, respectively. FeSO4, CuSO4, HgCl2, MnSO4 and MgSO4 did not inhibit the enzyme activity.