Enzyme immobilization on quercetin capped gold and silver nanoparticles for improved performance. (2019)

• Record Type: Journal Article
• Authors: Sanjana, S.; Medha, M.U.; Meghna, M.R.; Shruthi, T.S.; Srinivas, S.P.; Madhyastha, Harishkumar; Navya, P.N.; Daima, Hemant Kumar
• Is Part Of: Materials today. Volume 10:Part 1(2019)
• Page Start: 92
• Page End: 99
• Publication Date: 2019
• Subjects: Nanoparticles -- quercetin -- enzyme activity -- α-amylase -- immobilization; Materials science -- Congresses -- Periodicals; 620.1
• DOI: 10.1016/j.matpr.2019.02.193
• Languages: English
• ISSNs: 2214-7853

Abstract

Abstract: Recent development in the field of nanobiotechnology has gained importance due to its industrial applications, wherein the surface modification of nanoparticles with enzymes is of special interest. The enzyme immobilization strategies may advance the overall utility of the enzyme with improved performance. In this study, we illustrate the immobilization of enzyme "α-amylase" onto quercetin capped gold and silver nanoparticles without using any cross-linkers or additional surface alteration. The optimum pH and temperature for maximum enzyme activity for the immobilized amylase were estimated. The optimum pH for enzyme immobilized gold nanoparticles was found to be 6.5 and for silver nanoparticles it was found to be 4.5 and 8, whereas the ideal temperature for maximum amylase activity was 40°C and 50°C for gold and silver nanoparticles, respectively. The nanoparticles immobilized enzyme could retain over 50% of enzyme activity compare to 18% activity of free enzyme after six cycles. The outcome of the study indicates the ability of quercetin to reduce metal ions to form gold and silver nanoparticles with suitable surface corona to anchor amylase, and upon enzyme immobilization these nanoparticles can improve the performance of immobilized amylase toward pH, temperature and reusability compare to free enzyme