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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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Main Authors: Ong, Chong Boon, Annuar, Mohamad Suffian Mohamad
Format: Article
Published: Taylor & Francis 2018
Subjects:
Q Science (General)
QH Natural history
Online Access:http://eprints.um.edu.my/21073/
https://doi.org/10.1080/10826068.2018.1425707
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spelling 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
institution Universiti Malaya
building UM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Malaya
content_source UM Research Repository
url_provider http://eprints.um.edu.my/
topic Q Science (General)
QH Natural history
spellingShingle 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
description 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
url http://eprints.um.edu.my/21073/
https://doi.org/10.1080/10826068.2018.1425707
_version_ 1643691458950070272
score 13.18916

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