Influence of the use of Aliquat 336 in the immobilization procedure in sol–gel of lipase from Bacillus sp. ITP-001

Aliquat 336, a liquid hydrophobic material, was used at different concentrations (0.5–3.0%, w/v) as an additive in the preparation of encapsulated lipase from Bacillus sp. ITP-001 on sol–gel silica matrices using tetraethoxysilane (TEOS) as the precursor. The resulting hydrophobic matrices and immobilized lipases were characterized with regard to specific surface area (BET method), adsorption–desorption isotherms, pore volume (Vp) and size (dp) by nitrogen adsorption (BJH method) and scanning electron microscopy (SEM). The catalytic activities and the corresponding coupling yields were assayed in the hydrolysis of olive oil. In comparison with pure silica matrices, the immobilization process in the presence of Aliquat 336 decreased the values for specific surface area and increased the values for pore specific volume (Vp) and mean pore diameter (dp). This behavior may be related to the partial adsorption of the enzyme on the external surface of the hydrophobic matrix as indicated by scanning electron microscopy. Aliquat 336 concentrations in the range from 0.5 to 1.5% (w/v) provided immobilized derivatives with higher coupling yields and better substrate affinity. The highest coupling yield (YA = 71%) was obtained for the immobilized enzyme prepared in the presence of 1.5% Aliquat which gave the following morphological properties: specific surface area = 183 m2/g, pore specific volume (Vp) = 0.36 cc/g and mean pore diameter (dp) = 91 Å.

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► Aliquat 336 was used to protect the lipase from Bacillus sp. ITP-001 from inactivation during the immobilization procedure by the sol–gel technique.
► In the samples containing the enzyme and additive Aliquat (0.5–3.0%, w/v), the adsorbed volume was greater than that in pure silica.
► To enhance its applicability, immobilization was envisaged and the concentration of Aliquat 336 used here as an additive was evaluated in terms of the immobilized morphological structure and lipase activity recovery.