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• W1970313621 abstract "Immobilization of biologically important molecules on a myriad of nanosized materials has attracted great attention due to their small size, biocompatibility, higher surface-to-volume ratio, and lower toxicity. These properties make nanoparticles (NPs) a superior matrix over bulk material for the immobilization of enzymes and proteins. In the present study, Bacillus amyloliquefaciens α-amylase was immobilized on SnO2 nanoparticles by a simple adsorption mechanism. Nanoparticle-adsorbed enzyme retained 90% of the original enzyme activity. Thermal stability of nanosupport was investigated by thermogravimetric and differential thermal analysis. Scanning electron microscopic studies showed that NPs have porous structure for the high-yield immobilization of α-amylase. The genotoxicity of SnO2-NPs was analyzed by pUC19 plasmid nicking and comet assay and revealed that no remarkable DNA damage occurred in lymphocytes. The pH-optima was found to be the same for both free and SnO2-NPs bound enzyme, while the temperature-optimum for NPs-adsorbed α-amylase was 5°C higher than its free counterpart. Immobilized enzyme retained more than 70% enzyme activity even after its eight repeated uses." @default.
• W1970313621 created "2016-06-24" @default.
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• W1970313621 creator A5054008752 @default.
• W1970313621 date "2014-02-05" @default.
• W1970313621 modified "2023-09-26" @default.
• W1970313621 title "INFLUENCE OF pH AND TEMPERATURE ON THE ACTIVITY OF SnO₂-BOUND α-AMYLASE: A GENOTOXICITY ASSESSMENT OF SnO₂NANOPARTICLES" @default.
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• W1970313621 doi "https://doi.org/10.1080/10826068.2013.835732" @default.
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