Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8406251 | Biocatalysis and Agricultural Biotechnology | 2016 | 7 Pages |
Abstract
Ibead-CELipC12 is a metagenomic lipase, LipC12, immobilized directly from a crude extract onto Immobead 150. We evaluated its solvent and thermal stability and its potential for producing flavor esters and structured lipids. Ibead-CELipC12 had residual activities above 88% after 24 h at 40 °C in toluene, iso-octane, n-hexane and n-heptane and 72% after 24 h at 60 °C in n-hexane. In esterification of palmitic acid, Ibead-CELipC12 gave higher activities with ethanol, propanol and butanol than with isopropanol. In esterification of caprylic acid with ethanol, propanol and butanol, Ibead-CELipC12 performed best with butanol, giving 62% conversion in 6 h. Ibead-CELipC12 was sn-1,3-specific during triolein hydrolysis and was therefore used to convert olive oil into an MLM structured lipid containing 23% of caprylic acid in the sn-1 and sn-3 positions. These results demonstrate that Ibead-CELipC12 has good potential to be used in the enzymatic synthesis of flavor esters and structured lipids.
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Authors
Aline Dutra Madalozzo, Viviane Paula Martini, Keyla Kaori Kuniyoshi, Emanuel Maltempi de Souza, Fábio de Oliveira Pedrosa, Gisella Maria Zanin, David Alexander Mitchell, Nadia Krieger,