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

Dong M, Wu Z, Lu M, Wang Z, Li Z - Int J Mol Sci (2012)

Bottom Line: The property of amino-functionalized mesoporous silica was characterized by N(2) adsorption-desorption and thermogravimetric (TG) analysis.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.

View Article: PubMed Central - PubMed

Affiliation: Key Laboratory for Molecular Enzymology and Engineering of the Ministry of Education, College of Life Sciences, Jilin University, Changchun 130012, China; E-Mails: dong.meng.xing@163.com (M.D.); wuzf06@mails.jlu.edu.cn (Z.W.); luming@jlu.edu.cn (M.L.); wangzhi@jlu.edu.cn (Z.W.).

ABSTRACT
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.

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Schematic representation of the principle. First, the myoglobin was adsorbed into the channel of amino-functionalized mesoporous silica. Second, the lysozyme was linked to the external and internal surface of amino-functionalized mesoporous silica. The resulting product possessed two different enzymatic activities.
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f1-ijms-13-11443: Schematic representation of the principle. First, the myoglobin was adsorbed into the channel of amino-functionalized mesoporous silica. Second, the lysozyme was linked to the external and internal surface of amino-functionalized mesoporous silica. The resulting product possessed two different enzymatic activities.

Mentions: In order to overcome the leakage problem, two-step immobilization was carried out to achieve the immobilization of the enzyme in this experiment. Herein, myoglobin and lysozyme were selected as a model protein owing to its well known physicochemical property and commercial availability. First, amino-functionalized mesoporous molecular sieve was used to absorb myoglobin. Second, lysozyme was linked to the amino group of the amino-functionalized mesoporous molecular sieve to avoid the leaching of the absorbed myoglobin. Finally, the bifunctional bioreactor was obtained (Figure 1).


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

Dong M, Wu Z, Lu M, Wang Z, Li Z - Int J Mol Sci (2012)

Schematic representation of the principle. First, the myoglobin was adsorbed into the channel of amino-functionalized mesoporous silica. Second, the lysozyme was linked to the external and internal surface of amino-functionalized mesoporous silica. The resulting product possessed two different enzymatic activities.
© Copyright Policy - open-access
Related In: Results  -  Collection

License 1 - License 2
Show All Figures
getmorefigures.php?uid=PMC3472756&req=5

f1-ijms-13-11443: Schematic representation of the principle. First, the myoglobin was adsorbed into the channel of amino-functionalized mesoporous silica. Second, the lysozyme was linked to the external and internal surface of amino-functionalized mesoporous silica. The resulting product possessed two different enzymatic activities.
Mentions: In order to overcome the leakage problem, two-step immobilization was carried out to achieve the immobilization of the enzyme in this experiment. Herein, myoglobin and lysozyme were selected as a model protein owing to its well known physicochemical property and commercial availability. First, amino-functionalized mesoporous molecular sieve was used to absorb myoglobin. Second, lysozyme was linked to the amino group of the amino-functionalized mesoporous molecular sieve to avoid the leaching of the absorbed myoglobin. Finally, the bifunctional bioreactor was obtained (Figure 1).

Bottom Line: The property of amino-functionalized mesoporous silica was characterized by N(2) adsorption-desorption and thermogravimetric (TG) analysis.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.

View Article: PubMed Central - PubMed

Affiliation: Key Laboratory for Molecular Enzymology and Engineering of the Ministry of Education, College of Life Sciences, Jilin University, Changchun 130012, China; E-Mails: dong.meng.xing@163.com (M.D.); wuzf06@mails.jlu.edu.cn (Z.W.); luming@jlu.edu.cn (M.L.); wangzhi@jlu.edu.cn (Z.W.).

ABSTRACT
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.

Show MeSH
Related in: MedlinePlus