Combining the Physical Adsorption Approach and the Covalent Attachment Method to Prepare a Bifunctional Bioreactor

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 prop...

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Main Authors: Zhi Wang, Zhengqiang Li, Ming Lu, Zhuofu Wu, Mengxing Dong
Format: Article
Language:English
Published: MDPI AG 2012-09-01
Series:International Journal of Molecular Sciences
Subjects:
Online Access:http://www.mdpi.com/1422-0067/13/9/11443
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spelling doaj-183ce7d0b1b2450ab0d9b88c46143ad52020-11-24T21:04:44ZengMDPI AGInternational Journal of Molecular Sciences1422-00672012-09-01139114431145410.3390/ijms130911443Combining the Physical Adsorption Approach and the Covalent Attachment Method to Prepare a Bifunctional BioreactorZhi WangZhengqiang LiMing LuZhuofu WuMengxing DongAminopropyl-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 N2 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 H2O2 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.http://www.mdpi.com/1422-0067/13/9/11443adsorptionamino-functionalized mesoporous silicacovalent attachmentmyoglobinlysozymeperoxidase activityantibacterial activity
collection DOAJ
language English
format Article
sources DOAJ
author Zhi Wang
Zhengqiang Li
Ming Lu
Zhuofu Wu
Mengxing Dong
spellingShingle Zhi Wang
Zhengqiang Li
Ming Lu
Zhuofu Wu
Mengxing Dong
Combining the Physical Adsorption Approach and the Covalent Attachment Method to Prepare a Bifunctional Bioreactor
International Journal of Molecular Sciences
adsorption
amino-functionalized mesoporous silica
covalent attachment
myoglobin
lysozyme
peroxidase activity
antibacterial activity
author_facet Zhi Wang
Zhengqiang Li
Ming Lu
Zhuofu Wu
Mengxing Dong
author_sort Zhi Wang
title Combining the Physical Adsorption Approach and the Covalent Attachment Method to Prepare a Bifunctional Bioreactor
title_short Combining the Physical Adsorption Approach and the Covalent Attachment Method to Prepare a Bifunctional Bioreactor
title_full Combining the Physical Adsorption Approach and the Covalent Attachment Method to Prepare a Bifunctional Bioreactor
title_fullStr Combining the Physical Adsorption Approach and the Covalent Attachment Method to Prepare a Bifunctional Bioreactor
title_full_unstemmed Combining the Physical Adsorption Approach and the Covalent Attachment Method to Prepare a Bifunctional Bioreactor
title_sort combining the physical adsorption approach and the covalent attachment method to prepare a bifunctional bioreactor
publisher MDPI AG
series International Journal of Molecular Sciences
issn 1422-0067
publishDate 2012-09-01
description 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 N2 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 H2O2 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.
topic adsorption
amino-functionalized mesoporous silica
covalent attachment
myoglobin
lysozyme
peroxidase activity
antibacterial activity
url http://www.mdpi.com/1422-0067/13/9/11443
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