Abstract
The thermal stability of the purified lipase from Pseudomonas cepacia was investigated in both aqueous and organic media by using the “free” lipase and the lipase immobilised on Accurel EP-100. Both preparations were more stable in heptane than in water (597 and 240-fold for “free” and immobilised preparations, respectively). The first order inactivation constants were more sensitive to temperature changes (i.e. higher activation energy) for the “free” lipase than for the immobilised one.
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