Abstract
In order to improve the heat stability of purified lipase OF 360 from Candida cylindracea, lysine residues of the lipase were modified with a heterobifunctional photogenerated reagent, N-hydroxysuccinimide ester of 4-azidobenzoic acid, and photolyzed subsequently in the presence of decanol, which was proved to be a suitable heat stabilizer. The modified lipase showed excellent heat stability, even in the absence of decanol in the reaction system, compared to the native lipase. The activities of the modified lipase were retained about 70% after heating at 50°C for 15 min, while the native lipase lost about 80% of the original activities. The stabilization thus observed might be mainly caused by in situ formation of a cross-link between decanol and the lipase, and partly attributed to intra-molecular cross-linking in the lipase.
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