Abstract
Immobilized Aspergillus ficuum tannase on amino-functionalized multiwalled carbon nanotubes (A-MWCNT) was assembled through glutaraldehyde-mediated covalent coupling to produce a stable biocatalyst nanocomposite. The effective binding of tannase on the surface of A-MWCNT was evaluated and authenticated by spectroscopic signature signals and morphological differences, before and after enzyme coupling. Both free- and immobilized tannase showed optimal catalytic activities at pH 5.0 and 35 °C, with the immobilized tannase exhibiting enhanced thermostability compared to the soluble enzyme. The immobilized tannase preparation was also found to be reusable up to five cycles, with 66% of initial enzyme activity retained thereafter. The enzyme-carbon nanotube composite preparation allows for bioconversion to be accomplished in a bioreactor with a smaller footprint.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
