Purification lipoxygenase

Sekiya, J. Aoshima, H., Kajiwara, T., Togo, T. and Hatanaka, A. (1977). Purification and some properties of potato tuber lipoxygenase and detection of linoleic acid radical in the enzyme reaction. Agric. Biol. Chem. 41, 827-832. 

Perez-Gilabert M, Sanchez-Felipe I and Garcia-Carmona F. 2005. Purification and partial characterization of lipoxygenase from desert truffle (Terfezia claveryi Chatin) ascocarps. J Agric Food Chem 53(9) 3666-3671. 

Isolation, Purification, Characterization, and Assay of Antioxy-genic Enzymes Isolation and characterization of superoxide dis-mutase, 105, 88 superoxide dismutase assays, 105, 93 assays of glutathione peroxidase, 105, 114 catalase in vitro, 105, 121 assays of lipoxygenase, 105, 126. 

W-R Shieh. Part I. Studies on the active site-directed enzyme inhibitors of soybean lipoxygenase. Part n. Purification and studies on the [i-keto ester reductases from baker s yeast. Ph.D thesis. University of Wisconsin, Madison, WI, 1987. 

Considerable purification of lipoxygenase from soybeans was achieved by Balls et al (15), They used conventional protein purification methods and the carotene oxidase reaction to follow the enzyme activity. Theorell et al, (16), in 1947, crystallized the enzyme, or more correctly, one of the several isoenzymes in soybean. We believe this was lipoxygenase-1 as described later. 

Chen, A.O. and Whitaker, J.R., Purification and characterization of a lipoxygenase from immature English peas, J. Agric. Food Chem., 34, 203, 1986. 

Steczko, J. et al., Effect of ethanol and low temperature culture on expression of soybean lipoxygenase L-l in Escherichia coli, Prot. Express. Purif, 2, 221, 1991. 

The microbial lipoxygenase was purified using ultrafiltration. In this purification the specific activity of the enzyme preparation increased three times compared to the commercial preparation 2.214 E mg (U mg" ) and 860 E mg", respectively. 

Enzyme Purification. Broccoli contained sufficient levels of peroxidase, lipase and cystine lyase to permit their isolation in the amounts needed. Only traces of lipoxygenase and catalase were present. Activities (units/g vegetable see assay methods below) were peroxidase, 220 lipase, 12 lyase, 0.26. Catalase was M) units/g in broccoli compared to 19 in English green peas lipoxygenase was 2 units/g in broccoli compared to 110 in English green peas. Peroxidase, lipase and cystine lyase were purified by... 

Rapoport SM, Schewe T, Wiesner R, Halangk W, Ludwig P, Janicke-Hohne M, Tannert C, Hiebsch C, Klatt D. The lipoxygenase of reticulocytes. Purification, characterization and biological dynamics of the lipoxygenase its identity with the respiratory inhibitors of the reticulocyte. Eur J Biochem. 96 (1979) 545-561. 

Fornaroli, S. S. Petrussa E. Braidot A. Vianello F. Macri. Purification of a plasma membrane-bound lipoxygenase from soybean cotyledons. Plant Sci. 1999, 145, 1—10. 

Fukushige, H. C. Wang T.D. Simpson H.W. Gardner D.F. Hildebrand. Purification and identification of linoleic acid hydroperoxides generated by soybean seed lipoxygenases 2 and 3./. Agric. Food Chem. 2005, 53, 5691-5694. 

Rapoport, S M., Schewe, T., Wiesner, R., Halangk, W., Ludwig, P, Janicke-Hohne, M., Tannert, L., Hiebsch, C., and Klatt, D. (1979) The Lipoxygenase of Reticulocytes. Purification, Characterization and Biological Dynamics of the Lipoxygenase Its Identity with Respiratory Inhibitors of the Reticulocyte, Eur. J. Biochem. 96,545-561. 

The purification and characterization of a lipoxygenase-like enzyme in rat testis has also been described. The enzyme activity could be purified from the microsomes to almost homogeneity by affinity chromatography [203,204],... 

Soybean type-I lipoxygenase is particularly stable. Other lipoxygenases are less stable and activity is lost during purification. Heat treatment is often used in the food industry to cause inactivation so as to prevent off-flavours. The purified lipoxygenases are generally unstable at 70 °C but higher temperatures may be necessary for inactivating the enzymes in foodstuffs. 

Lipoxygenases from different sources differ in their cooxidation activity. Enzymes from peas and beans (Phaseolus sp.) and the LOX-2 from soybean have a high cooxidation potential potato LOX is intermediate, whereas wheat, flax, and soybean LOX-1 have poor cooxidation activity (Grosch et al., 1976, 1977). Thus, the carotene oxidase activity of soybeans is associated with the LOX-2 isoenzyme, and this explains the observed selective loss of carotenoid bleaching activity during the purification and heat treatment of the classic (i.e., LOX-1) enzyme from soybean (Kies et al., 1969). 

Battu, S., Rabinovitch-Chable, H. And Beneytout, J. L. (1994) Effectiveness of talc as adsorbent for purification and immobilization of plant lipoxygenases, J. Agric. Food Chem. Vol. 42, 2115-2112. 

SUBSTRATE SPECIFICITY OF BARLEY LIPOXYGENASE ISOENZYMES Purification oflox-1 and lox-2... 

Doderer A., KokkelinkL, van der Veen S., ValkB.E., Schram A.W. and Douma A.C. (1992) Purification and characterization of two lipoxygenase isoenzymes from germinating barley, Biochim. Biophys. Acta 1120, 97-104. 

Yang G., Schwarz P.B. and Vick B. A. (1993) Purification and characterization of lipoxygenase isoenzymes in germinating barley, Afti. Assoc. Cereal Chem. 70 (5) 589-595. 

Nicholas, J., Autran, M. and Dapron, R. (1982) Purification and some properties of wheat germ lipoxygenase. J. Sci. Food. Agric. 33, 365-372. 

Recent work has revealed that lipoxygenases from some plant tissues oxidize a-ketols of a-linolenic acid to hydroperoxides of a-ketols [3]. This paper deals with the formation of similar products by the other way by hydroperoxide dehydration of double dioxygenation products. Incubation of 9-hydroxy-16-hydroperoxy-10( ),12(Z),14( )-[l-l C]octadecatrienoic acid with enzyme preparation from com seeds led to the formation of three polar metabolites. After RP- and SP-HPLC purifications two of these polar metabolites were identified by UV spectroscopy and electron-impact mass spectrometry as a- and y-ketols of 9-hydroxy derivative of a-linolenic acid 9,16-dihydroxy-15-oxo-I0(, 12(Z)-octadecadienoic acid and 9,12-dihydroxy-15-oxo-I0(jE, 13( )-octadecadienoic acid, respectively. Stmcture of the most polar metabolite is discussed. 

Fournier J, Pouenat ML, Rickauer M, Rabinovitch-Chable H, Rigaud M, Esquerre-Tugay MT Purification and characterization of elicitor-induced lipoxygenase in tobacco cells. Plant J 1993 3 63-70. 

Van Aarle PGM, De Barse MMJ, Veldink GA, Vliegenthart JFG. Purification of a lipoxygenase from ungerminated barley. Characterization and product formation. FEBS Lett 1991 280 159-62. 

Narumiya S, Salmon SA, Cottee FH, Weatherly BC, Flower RJ. Arachidonic acid 15-lipoxygenase from rabbit peritoneal polymorphonuclear leukocytes. Partial purification and properties. J Biol Chem 1981 256 9583-9592. 

Izumi T, Radmark O, Jornvall H, Samuelsson B. Purification of two forms of arachidonate 15-lipoxygenase from human leukocytes. Eur J Biochem 1991 202 1231-1238. 

---