Immobilization of cross-linked tannase enzyme on multiwalled carbon nanotubes and its catalytic behavior
Document Type
Article
Publication Date
1-1-2018
Abstract
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.
Keywords
Glutaraldehyde, immobilization, multiwalled carbon nanotubes, tannase
Divisions
InstituteofBiologicalSciences
Funders
University of Malaya: Postgraduate Research Grant (PG033-2013A) and UMRG (RP031C-15AET)
Publication Title
Preparative Biochemistry and Biotechnology
Volume
48
Issue
2
Publisher
Taylor & Francis
Additional Information
http://orcid.org/0000-0003-4564-6043