1 research outputs found
Fabrication of Lignosulfonate Vesicular Reverse Micelles to Immobilize Horseradish Peroxidase
Sodium lignosulfonate reverse micelles
(SLRMs) with vesicular structure
were prepared by self-assembling in ethanol–water media and
applied to encapsulate horseradish peroxidase (HRP). Results showed
that sodium lignosulfonate (SL) could not form SLRMs until the ethanol
content reached 63% when its initial concentration was 7.5 g L<sup>–1</sup>. Owing to strong electrostatic repulsion, solid spherical
SLRMs gradually swelled to stable vesicular structures with an average
size of 240 nm. The shell of the SLRM thickened when NaCl was added
to screen the electrostatic interaction. HRP can be effectively encapsulated
while retaining its activity in the hydrophilic core of a SLRM. When
hydrogen peroxide was added to initiate the catalytic activity of
HRP, SL molecules would be polymerized and the structure of SLRMs
would be fixed. Furthermore, HRP immobilized in polymerized SLRMs
showed high activity at a more acidic pH of 4 and at a lower optimal
temperature decrease of 35 °C compared to free HRP. SLRM allows
enzymes such as HRP to work at more acidic and lower temperature conditions