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Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/34684
Title: Oxidative degradation of model lipids representative for main paper pulp lipophilic extractives by the lacasse-mediator system
Authors: Molina, Setefilla ; Rencoret, Jorge ; Río Andrade, José Carlos del ; Lomascolo, Anne; Record, Éric; Martínez, Ángel T.; Gutiérrez Suárez, Ana
Keywords: Laccase-mediator system
fungal enzymes
model lipids
reaction mechanisms
paper pulps
pitch deposits
Issue Date: 2008
Publisher: Springer
Citation: Applied Microbiology and Biotechnology 80:211-222 (2008)
Abstract: Different model lipids—alkanes, fatty alcohols, fatty acids, resin acids, free sterols, sterol esters, and triglycerides—were treated with Pycnoporus cinnabarinus laccase in the presence of 1-hydroxybenzotriazole as mediator, and the products were analyzed by gas chromatography. The laccase alone decreased the concentration of some unsaturated lipids. However, the most extensive lipid modification was obtained with the laccase–mediator system. Unsaturated lipids were largely oxidized and the dominant products detected were epoxy and hydroxy fatty acids from fatty acids and free and esterified 7-ketosterols and steroid ketones from sterols and sterol esters. The former compounds suggested unsaturated lipid attack via the corresponding hydroperoxides. The enzymatic reaction on sterol esters largely depended on the nature of the fatty acyl moiety, i.e., oxidation of saturated fatty acid esters started at the sterol moiety, whereas the initial attack of unsaturated fatty acid esters was produced on the fatty acid double bonds. In contrast, saturated lipids were not modified, although some of them decreased when the laccase–mediator reactions were carried out in the presence of unsaturated lipids suggesting participation of lipid peroxidation radicals. These results are discussed in the context of enzymatic control of pitch to explain the removal of lipid mixtures during laccase–mediator treatment of different pulp types.
Description: E-mail: anagu@irnase.csic.es (A. Gutiérrez)
URI: http://hdl.handle.net/10261/34684
DOI: http://dx.doi.org/10.1007/s00253-008-1547-6
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