ORANGE WASTES: DIRECT LIPASE SOURCE

The research aims to obtain specific activity of lipase from the direct form, using the plant itself for this purpose, in orange residues (Citrus sinensis L. Osbeck). These residues (bagasse, peel and frit) were wash, lyophilize and made its bromatological characterization. The determination of enzymatic activity was order by titration, p-NPB (p-nitrophenylbutyrate), to quantify of short chain fatty acids, and p-NPP (p-nitrophenylpalmitate), to analyze of long chain fatty acids. The enzyme unit for both was stipulate as the amount of enzyme require to release 1 μmol of p-nitrophenol per minute of reaction. The analyses of total proteins were perform in order to determine specific activity. Wastes showed lipase activities in all parts (48.59 U/g), that can be due of similar presence in their lipid composition (0.11%). The high moisture (72.36%) ensures the water-oil interface required to promote lipase action. The best specific activity obtained was bagasse lipase (561.04 U/mg), in breaking of short chain fatty acid (p<0.05). For the lipolytic activity, bagasse was also highlighted to butyrate (497.64 U/g) and (10.54 U/g) palmitate. Thus, the orange wastes showed to be promising to obtaining lipases, which had specificity for the breaking short chains of fatty acids.