Immobilisation of lipases by adsorption and deposition: high protein loading gives lower water activity optimum |
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Authors: | Mattias Persson Ernst Wehtje Patrick Adlercreutz |
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Affiliation: | (1) Department of Biotechnology, Center for Chemisty and Chemical Engineering, Lund University, P.O. Box 124, S-221 00 Lund, Sweden |
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Abstract: | Two different immobilisation techniques for lipases were investigated: adsorption on to Accurel EP-100 and deposition on to Celite. The specific activities were in the same order of magnitude, 2.9 (mol min–1 mg protein) when Celite was used as support and 2.3 (mol min–1 mg–1 protein) when Accurel EP-100 was used as support, even if the amount of lipase loaded differed by 2 orders of magnitude. Immobilisation on Accurel EP-100 was the preferred technique since 40–100 times more protein can be loaded/per g carrier, thus yielding a more active catalyst. The water activity profiles in lipase catalysed esterification were influenced by the amount of protein adsorbed to Accurel EP-100. Higher protein loading (40 mg g–1) resulted in a bell-shaped water activity profile with highest specific activity (6.1 mol min–1 mg–1 protein) at aw=0.11, while an enzyme preparation with low protein loading (4 mg g–1) showed highest specific activity at aw=0.75. |
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Keywords: | Immobilisation lipase protein loading water activity |
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