Characterisation of lipoxygenase from pea seeds (Pisum sativum var. Telephone L.) |
| |
Authors: | Urszula Szymanowska Anna JakubczykBarbara Baraniak Agnieszka Kur |
| |
Affiliation: | Department of Biochemistry and Food Chemistry, University of Life Sciences, ul. Skromna 8, 20-704 Lublin, Poland |
| |
Abstract: | Lipoxygenase (LOX) from pea seeds (Pisum sativum var. Telephone L.) was extracted and studied of biochemical properties. The molecular mass of purified lipoxygenase was 93 kDa. The effects of substrate specificity, pH, and sensibility to various inhibitors: caffeic acid, ferulic acid, benzoic acid, catechin, quercetin and kaempferol of LOX were investigated. Lipoxygenase showed the highest activity toward linoleic acid and the lowest toward oleic acid as substrates. Kinetic studies indicated that Vmax of the LOX activity was 151.5 U/min and corresponding Km value of 0.44 × 10−3 M. Optimum pH of lipoxygenase was reported at 5.5. Caffeic acid was the most effective inhibitor and kaempferol was the least effective. |
| |
Keywords: | Lipoxygenase Pisum sativum Purification Characterisation Linoleic acid |
本文献已被 ScienceDirect 等数据库收录! |
|