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Updated: Apr 16, 2026

Microfluidic Production of Lysolipid-Containing Temperature-Sensitive Liposomes
Published on: March 3, 2020
AOT/isooctane reverse micelles with a microaqueous core act as protective shells for enhancing the thermal stability
Sung-Chul Hong1, Kyung-Min Park1, Young-Hwan Son2
1Department of Agricultural Biotechnology, Seoul National University, Seoul 151-921, Republic of Korea.
Abstract:
According to the different environmental systems for lipase reactions, changes in thermal stability were investigated by employing the Chromobacterium viscosum lipase and a two-step series-type deactivation model. The half-life (6.81 h) of the lipase entrapped in reverse micelles at 70 °C was 9.87- and 14.80-fold longer than that in glycerol pool or in aqueous buffer. The deactivation constants for the first and second step (k1 and k2) at all temperatures drastically decreased when the lipase was entrapped in reverse micelles. In particular, k1 (3.84 h(-1)) at 70 °C in reverse micelles was 1.57-fold lower than that in aqueous buffer (6.03 h(-1)). Based on the fluorescence spectrometry, the amount of excited forms of tryptophan and tyrosine increased markedly during the thermal-treatment in aqueous buffer, whereas no significant fluctuation was noted in the reversed micellar system. These results indicated that the encapsulation in reverse micelles could be favorable for preventing the enzyme from heat-induced denaturation.
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