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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

Fourier transform infrared (FTIR) spectra of amino-functionalized mesoporous silica (heavy line) and the sample after myoglobin adsorption (fine line).
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f4-ijms-13-11443: Fourier transform infrared (FTIR) spectra of amino-functionalized mesoporous silica (heavy line) and the sample after myoglobin adsorption (fine line).

Mentions: In FTIR spectra, the broad peak at around 3500 cm−1 was assigned to the stretch vibration of N–H (Figure 4). Three absorbance peaks in the range of 2800–3000 cm−1 were associated with stretching and bending vibration of C–H. Two negative peaks at 2200–2400 cm−1 were attributed to the contribution of CO2 in the environment. The absorption peak at 1630 cm−1 might be due to bending vibration of the adsorbed water molecules. The formation of polysiloxane was confirmed by the Si-O-Si band at 804 cm−1. The incorporation of the amino group was verified by symmetric –NH2 bending vibration at 1515 cm−1 [17].


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)

Fourier transform infrared (FTIR) spectra of amino-functionalized mesoporous silica (heavy line) and the sample after myoglobin adsorption (fine line).
© Copyright Policy - open-access
Related In: Results  -  Collection

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

f4-ijms-13-11443: Fourier transform infrared (FTIR) spectra of amino-functionalized mesoporous silica (heavy line) and the sample after myoglobin adsorption (fine line).
Mentions: In FTIR spectra, the broad peak at around 3500 cm−1 was assigned to the stretch vibration of N–H (Figure 4). Three absorbance peaks in the range of 2800–3000 cm−1 were associated with stretching and bending vibration of C–H. Two negative peaks at 2200–2400 cm−1 were attributed to the contribution of CO2 in the environment. The absorption peak at 1630 cm−1 might be due to bending vibration of the adsorbed water molecules. The formation of polysiloxane was confirmed by the Si-O-Si band at 804 cm−1. The incorporation of the amino group was verified by symmetric –NH2 bending vibration at 1515 cm−1 [17].

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