Covalent Immobilization of Cellulase in Application of Biotransformation of Ginsenoside Rb1

Publication date: Available online 11 May 2017 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Ying Yuan, Xiaoning Luan, Mohamed E. Hassan, Deqiang Dou Cellulase was immobilized on the surface of carrageenan beads activated by using polyethyleneimine and glutaraldehyde, then immobilized cellulase was used to transform ginsenoside Rb1. In this work, we studied the functionalization of carrageenan with amine terminal functional group for the covalent immobilization of cellulase. The process of immobilization was performed by amination process on the surface of the carrageenan gel beads with polyethylenimine followed by activation with glutaraldehyde to finally immobilize the enzyme. Different factors affecting the amination and activation processes were studied and their effects on the catalytic activity of the immobilized cellulase were followed, then Fourier transform infrared spectroscopy and scanning electron microscopy were applied to verify the process. Furthermore, the optimum conditions of transformation of ginsenoside Rb1 were also studied and showed better stability for the immobilized enzyme. The best results were obtained using carrageenan as support and covalent binding method, which consisted of amination process (0.5% PEI (pH 8) for 3h and 3% GA in activation process for 3h. These experiments gave optimum reaction condition of temperature at 60°C and pH 5.0. Enzyme after immobilization exhibited high activity with broader pH and temperature r...

Source: Journal of Molecular Catalysis B: Enzymatic - May 11, 2017 Category: Biochemistry Source Type: research