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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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Related in: MedlinePlus

UV/VIS spectra of product produced by adsorbed myoglobin (a); amino-functionalized mesoporous silica (b) and amino-functionalized mesoporous silica linked by lysozyme without myoglobin (c).
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f6-ijms-13-11443: UV/VIS spectra of product produced by adsorbed myoglobin (a); amino-functionalized mesoporous silica (b) and amino-functionalized mesoporous silica linked by lysozyme without myoglobin (c).

Mentions: After adsorption, lysozyme was covalently tethered to the surface of glutaraldehyde activated amino-functionalized mesoporous silica. The aldehyde group of the glutaraldehyde molecule connected with the amino group of amino-functionalized mesoporous silica and lysozyme through Schiff’s base reaction [26]. As can be seen from Figure 6, the absorbance peak of the produced bisazobiphenyl appeared at 472 nm, which was in accordance with the result of Claiborne and coworkers [27], suggesting that the adsorbed myoglobin still exhibited peroxidative activity after covalent attachment of lysozyme.


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)

UV/VIS spectra of product produced by adsorbed myoglobin (a); amino-functionalized mesoporous silica (b) and amino-functionalized mesoporous silica linked by lysozyme without myoglobin (c).
© Copyright Policy - open-access
Related In: Results  -  Collection

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

f6-ijms-13-11443: UV/VIS spectra of product produced by adsorbed myoglobin (a); amino-functionalized mesoporous silica (b) and amino-functionalized mesoporous silica linked by lysozyme without myoglobin (c).
Mentions: After adsorption, lysozyme was covalently tethered to the surface of glutaraldehyde activated amino-functionalized mesoporous silica. The aldehyde group of the glutaraldehyde molecule connected with the amino group of amino-functionalized mesoporous silica and lysozyme through Schiff’s base reaction [26]. As can be seen from Figure 6, the absorbance peak of the produced bisazobiphenyl appeared at 472 nm, which was in accordance with the result of Claiborne and coworkers [27], suggesting that the adsorbed myoglobin still exhibited peroxidative activity after covalent attachment of lysozyme.

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