Purification and characterization of a lipoxygenase enzyme from durum wheat semolina.

  title={Purification and characterization of a lipoxygenase enzyme from durum wheat semolina.},
  author={R. Barone and R. Briante and S. d'Auria and F. Febbraio and C. Vaccaro and L. Del Giudice and G. M. Borrelli and N. Di Fonzo and R. Nucci},
  journal={Journal of agricultural and food chemistry},
  volume={47 5},
Purification of a lipoxygenase enzyme from the cultivar Tresor of durum wheat semolina (Triticum turgidum var. durum Desf) was reinvestigated furnishing a new procedure. The 895-fold purified homogeneous enzyme showed a monomeric structure with a molecular mass of 95 +/- 5 kDa. Among the substrates tested, linoleic acid showed the highest k(cat)/K(m) value; a beta-carotene bleaching activity was also detected. The enzyme optimal activity was at pH 6. 8 on linoleic acid as substrate and at pH 5… Expand
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