Immobilization of horseradish peroxidase on β-cyclodextrin-capped silver nanoparticles

Its future aspects in biosensor application

Document identifier: oai:DiVA.org:ltu-7633
Access full text here:10.1080/10826068.2015.1031389
Keyword: Engineering and Technology, Industrial Biotechnology, Bio Materials, Teknik och teknologier, Industriell bioteknik, Biomaterial, Trä och bionanokompositer, Wood and Bionanocomposites
Publication year: 2016
Relevant Sustainable Development Goals (SDGs):
SDG 3 Good health and wellbeing
The SDG label(s) above have been assigned by OSDG.ai

Abstract:

This study aimed to work out a simple and high-yield procedure for the immobilization of horseradish peroxidase on silver nanoparticle. Ultraviolet–visible (UV-vis) and Fourier-transform infrared spectroscopy and transmission electron microscopy were used to characterize silver nanoparticles. Horseradish peroxidase was immobilized on β-cyclodextrin-capped silver nanoparticles via glutaraldehyde cross-linking. Single-cell gel electrophoresis (Comet assay) was also performed to confirm the genotoxicity of silver nanoparticles. To decrease toxicity, silver nanoparticles were capped with β-cyclodextrin. A comparative stability study of soluble and immobilized enzyme preparations was investigated against pH, temperature, and chaotropic agent, urea. The results showed that the cross-linked peroxidase was significantly more stable as compared to the soluble counterpart. The immobilized enzyme exhibited stable enzyme activities after repeated uses.

Authors

Zoheb Karim

Luleå tekniska universitet; Materialvetenskap
Other publications >>

Mohd Jahir Khan

School of Chemical Sciences and Food Technology, Faculty of Science and Technology, Universiti Kebangsaan Malaysia, Bangi
Other publications >>

Mohamad Yusof Maskat

School of Chemical Sciences and Food Technology, Faculty of Science and Technology, Universiti Kebangsaan Malaysia, Bangi
Other publications >>

Rohana Adnan

School of Chemical Sciences, Universiti Sains Malaysia, Minden Penang
Other publications >>

Record metadata

Click to view metadata