Lipoxygenase from baker's yeast: Purification and properties

Abstract

1. 1. Lipoxygenase activity was extracted from the mitochondrial fraction of baker's yeast and was purified by affinity chromatography on a linoleyl aminoethyl sepharose column. Two lipoxygenases were eluted from the affinity column. 2. 2. The second enzyme eluted was characterized as a true lipoxygenase. 3. 3. The lipoxygenase eluted showed maximum activity at pH 6.5 with a K m of 2.68 × 10 −4 M on linoleate. 4. 4. The reaction products of the second lipoxygenase with linoleate were characterized by u.v., i.r., NMR spectra and mass spectrometry and were found to be: 9-hydroperoxy-octadeca- trans-10, cis-12-dienoic acid and 13-hydroperoxy-octadeca- cis-9, trans-11-dienoic acid.