Abstract
AbstractThis study reports the purification and characterization of lipoxygenase protein from walnut (Juglans regia). Lipoxygenases (LOX) are the key enzyme of germination in plants. Purification of LOX was 62,28 fold in 68 % yield with a specific activity of 24.29 U/mg using ammonium sulfate precipitation and DEAE‐Sepharose Fast Flow Ion Exchange Column. The optimum pH value of the enzyme was determined as pH 7 and the optimum temperature value as 30 °C. It was determined that morin hydrate, p‐coumaric acid, syringaldehyde and vanillic acid inhibited LOX, and their IC50 values were 304 μM, 233 μM, 643.2 μM and 218.1 μM respectively. It has been concluded that walnut, which is used frequently in many parts of the world, is a good source of LOX and this study can be a guide for studies in medicine, food industry, cosmetics and pharmacy.
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