Combining the physical adsorption approach and the covalent attachment method to prepare a bifunctional bioreactor

• Published in: International journal of molecular sciences Vol. 13; no. 9; pp. 11443 - 11454
• Main Authors: Dong, Mengxing, Wu, Zhuofu, Lu, Ming, Wang, Zhi, Li, Zhengqiang
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 01.09.2012; Molecular Diversity Preservation International (MDPI)
• Subjects: Adsorption; amino-functionalized mesoporous silica; Anti-Bacterial Agents - metabolism; antibacterial activity; Bioreactors; covalent attachment; Dianisidine - metabolism; Enzymes; Experiments; Fourier transforms; Glutaral - chemistry; Hydrogen Peroxide - metabolism; Lactose; lysozyme; Micrococcus - metabolism; Muramidase - chemistry; myoglobin; Myoglobin - metabolism; peroxidase activity; Peroxidases - metabolism; Pore size; Silicon Dioxide - chemistry; Spectroscopy, Fourier Transform Infrared; antibacterial activity; amino-functionalized mesoporous silica; peroxidase activity; adsorption; lysozyme; covalent attachment; myoglobin
• ISSN: 1422-0067; 1661-6596; 1422-0067
• DOI: 10.3390/ijms130911443

Aminopropyl-functionalized SBA-15 mesoporous silica was used as a support to adsorb myoglobin. Then, in order to avoid the leakage of adsorbed myoglobin, lysozyme was covalently tethered to the internal and external surface of the mesoporous silica with glutaraldehyde as the coupling agent. The property of amino-functionalized mesoporous silica was characterized by N(2) adsorption-desorption and thermogravimetric (TG) analysis. The feature of the silica-based matrix before and after myoglobin adsorption was identified by fourier transform infrared (FTIR) and UV/VIS measurement. With o-dianisidine and H(2)O(2) as the substrate, the peroxidase activity of adsorbed myoglobin was determined. With Micrococus lysodeilicus as the substrate, the antibacterial activity of covalently tethered lysozyme was measured. Results demonstrated that the final product not only presented peroxidase activity of the myoglobin but yielded antibacterial activity of the lysozyme.