Immobilization of cross-linked tannase enzyme on multiwalled carbon nanotubes and its catalytic behavior
Immobilization of cross-linked tannase on pristine multiwalled carbon nanotubes (MWCNT) was successfully performed. Cross-linking of tannase molecules was made through glutaraldehyde. The immobilized tannase exhibited significantly improved pH, thermal, and recycling stability. The optimal pH for bo...
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my.um.eprints.210732019-04-25T03:16:15Z http://eprints.um.edu.my/21073/ Immobilization of cross-linked tannase enzyme on multiwalled carbon nanotubes and its catalytic behavior Ong, Chong Boon Annuar, Mohamad Suffian Mohamad Q Science (General) QH Natural history Immobilization of cross-linked tannase on pristine multiwalled carbon nanotubes (MWCNT) was successfully performed. Cross-linking of tannase molecules was made through glutaraldehyde. The immobilized tannase exhibited significantly improved pH, thermal, and recycling stability. The optimal pH for both free and immobilized tannase was observed at pH 5.0 with optimal operating temperature at 30°C. Moreover, immobilized enzyme retained greater biocatalytic activities upon 10 repeated uses compared to free enzyme in solution. Immobilization of tannase was accomplished by strong hydrophobic interaction most likely between hydrophobic amino acid moieties of the glutaraldehyde-cross-linked tannase to the MWCNT. Taylor & Francis 2018 Article PeerReviewed Ong, Chong Boon and Annuar, Mohamad Suffian Mohamad (2018) Immobilization of cross-linked tannase enzyme on multiwalled carbon nanotubes and its catalytic behavior. Preparative Biochemistry and Biotechnology, 48 (2). pp. 181-187. ISSN 1082-6068 https://doi.org/10.1080/10826068.2018.1425707 doi:10.1080/10826068.2018.1425707 |
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Q Science (General) QH Natural history Ong, Chong Boon Annuar, Mohamad Suffian Mohamad Immobilization of cross-linked tannase enzyme on multiwalled carbon nanotubes and its catalytic behavior |
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Immobilization of cross-linked tannase on pristine multiwalled carbon nanotubes (MWCNT) was successfully performed. Cross-linking of tannase molecules was made through glutaraldehyde. The immobilized tannase exhibited significantly improved pH, thermal, and recycling stability. The optimal pH for both free and immobilized tannase was observed at pH 5.0 with optimal operating temperature at 30°C. Moreover, immobilized enzyme retained greater biocatalytic activities upon 10 repeated uses compared to free enzyme in solution. Immobilization of tannase was accomplished by strong hydrophobic interaction most likely between hydrophobic amino acid moieties of the glutaraldehyde-cross-linked tannase to the MWCNT. |
format |
Article |
author |
Ong, Chong Boon Annuar, Mohamad Suffian Mohamad |
author_facet |
Ong, Chong Boon Annuar, Mohamad Suffian Mohamad |
author_sort |
Ong, Chong Boon |
title |
Immobilization of cross-linked tannase enzyme on multiwalled carbon nanotubes and its catalytic behavior |
title_short |
Immobilization of cross-linked tannase enzyme on multiwalled carbon nanotubes and its catalytic behavior |
title_full |
Immobilization of cross-linked tannase enzyme on multiwalled carbon nanotubes and its catalytic behavior |
title_fullStr |
Immobilization of cross-linked tannase enzyme on multiwalled carbon nanotubes and its catalytic behavior |
title_full_unstemmed |
Immobilization of cross-linked tannase enzyme on multiwalled carbon nanotubes and its catalytic behavior |
title_sort |
immobilization of cross-linked tannase enzyme on multiwalled carbon nanotubes and its catalytic behavior |
publisher |
Taylor & Francis |
publishDate |
2018 |
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http://eprints.um.edu.my/21073/ https://doi.org/10.1080/10826068.2018.1425707 |
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1643691458950070272 |
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13.18916 |