Active biocatalysts based on Candida rugosa lipase immobilized in vesicular silica

Abstract

Vesicular silica (VS) with hierarchical structure was prepared by utilizing cationic surfactant cetyltrimethylammonium bromide (CTAB) and anionic surfactant sodium dodecyl sulfate (SDS) as the structure directing agents, and 1,3,5-triisopropylbenzene (TIPB) as the micelle expander. The resulting unilamellar and multilamellar VS with interlamellar mean mesopore size of 15–20nm and shell thickness of 5–15nm were used as supports for immobilization of Candida rugosa lipase (CRL) through physical adsorption. Possible mechanisms for the formation of VS and the immobilization of CRL on VS are proposed. N2 adsorption-desorption experiments and Fourier transform infrared spectroscopy (FT-IR) measurements demonstrated that CRL was adsorbed into the curved channels of the VS. The catalytic activity, thermal stability, and reusability of VS immobilized CRL were assayed in phosphate buffer medium by hydrolysis of triacetin. The effects of pH and temperature on enzyme activity were also investigated. We report that VS immobilized CRL exhibited outstanding adaptability at higher pH and temperature, and excellent thermal stability and reusability compared with free CRL.