The lipoxygenase isoenzymes LOX1 and LOX2 from green malt were separated by isoelectric focusing, and their catalytic properties regarding complex lipids as substrates were characterized. The regio- and stereoisomers of hydroperoxy octadecadienoates (HPODE) resulting from LOX1 and LOX2 enzymatic transformations of linoleic acid, methyl linoleate, linoleic acid glycerol esters monolinolein, dilinolein, and trilinolein, and 1-palmitoyl-2-linoleoyl-glycero-3-phosphocholine (PamLinGroPCho) were determined. In addition, biotransformations of polar and nonpolar lipids extracted from malt were performed with LOX1 and LOX2. The results show that LOX2 catalyzes the oxidation of esterified fatty acids at a higher rate and is more regioselective than LOX1. The dual position specificity of LOX2 (9-HPODE:13-HPODE) with trilinolein as the substrate (6:94) was higher than the resultant ratio (13:87) when free linoleic acid was transformed. A high (S)-enantiomeric excess of 13-HPODE was analyzed with all esterified substrates confirming the formation of 13-HPODE through the LOX2 enzyme; however, 9-HPODE detected after LOX2 biotransformations showed (R)-enantiomeric excesses. PamLinGroPCho was oxygenated by LOX1 with the highest regio- and stereoselectivities among the applied substrates.

The characterisation of lipoxygenases LOX1 and LOX2 and hydroperoxyoctadecadienoic acid (HPODE) degrading enzymes from barley green malt is reported. Hydroxylapatite chromatography (HAC) and isoelectric focussing (IEF) were performed to separate and purify LOX isoenzymes. The regio-and stereoselectivity of LOX1 and LOX2 towards linoleic acid as substrate was characterised. HAC purified isoenzyme LOX1 showed a 9-HPODE:13-HPODE ratio of 75:25 and LOX2 a ratio of 39:61. IEF separated LOX1 and LOX2 transformed linoleic acid to 9-:13-HPODE ratios of 90:10, and 13:87, respectively. 9-HPODE stereoisomers from LOX1 exhibited a S:R ratio of 93:7 and 13-HPODE from LOX2 a S:R ratio of 89:11. However, the minor regioisomers were analysed with S:R = 48:52 (LOX1, 13-HPODE) and 40:60 (LOX2, 9-HPODE). These results indicate a complete LOX isoenzyme separation by IEF. Hydroperoxide-metabolising enzymes, which were investigated in the IEF fractions, did not interfere with the dual position specificities of LOX isoenzymes.

Brazil has been presenting in the last years a scientific production well-recognized in the international scenario, in several areas of knowledge, according to the impact of their publications in important events and especially in indexed journals of wide circulation. On the other hand, the country does not seem to be in the same direction regarding to the technological production and wealth creation from the established scientific development, and particularly from the applied research. The present paper covers such issue and discloses the main similarities and differences between a scientific paper and a patent application, in order to contribute to a better understanding of both types of documents and help the researchers to chose and select the results with technological potential, decide what is appropriated for industrial protection, as well as foster new business opportunities for each technology which has been created.