Kinetics of adsorption of lipase onto different mesoporous materials: Evaluation of Avrami model and leaching studies

• Mesoporous silica supports having different pore diameter and morphology was synthesized by changing auxiliary chemical.
• Kinetic parameters were estimated by Avrami model for different supports to make a perfect correlation with the kinetics of enzyme adsorption.
• The enzyme immobilized via covalent binding onto MCF-25G showed higher activity and stability due to special morphology and high porosity.
• Leaching studies revealed that covalent bound enzyme was less prone to leaching.

Mesoporous silica materials were synthesized by hydrothermal route and covalently modified with glutaraldehyde. The adsorption (chemical adsorption and physical adsorption) of enzyme Candida rugosa lipase onto pure and functionalized mesoporous silica materials having different pore diameter were studied. Kinetics of adsorption was evaluated by Avrami model and specific kinetic parameters n and k were determined experimentally. Leaching studies revealed that chemical adsorption via covalent binding was less prone to leaching. Maximum loading capacity of each mesoporous material was analyzed and the result showed that MCF-25G has highest adsorption capacity. It was also observed that MCF-25G has highest stability towards enzyme binding.

Kinetics of protein adsorption on different mesoporous materials.Figure optionsDownload as PowerPoint slide