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- W2059411703 abstract "Proteins adsorbed on nanoparticles (NPs) are being used in biotechnology, biosensors and drug delivery. However, understanding the effect of NPs on the structure of proteins is still in a nascent state. In the present paper tin oxide (SnO2) NPs were synthesized by the reaction of SnCl4·5H2O in methanol via the sol–gel method and characterized by x-ray diffraction (XRD), Fourier transform infrared spectroscopy (FT-IR) and transmission electron microscopy (TEM). The binding of these SnO2–NPs with α-amylase was investigated by using UV–vis, fluorescence and circular dichroism (CD) spectroscopic techniques. A strong quenching of tryptophan fluorescence intensity in α-amylase was observed due to formation of a ground state complex with SnO2–NPs. Far-UV CD spectra showed that the secondary structure of α-amylase was changed in the presence of NPs. The Michaelis–Menten constant (Km), was found to be 26.96 and 28.45 mg ml − 1, while Vmax was 4.173 and 3.116 mg ml − 1 min − 1 for free and NP-bound enzyme, respectively." @default.
- W2059411703 created "2016-06-24" @default.
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- W2059411703 date "2011-10-21" @default.
- W2059411703 modified "2023-09-23" @default.
- W2059411703 title "Effect of tin oxide nanoparticle binding on the structure and activity of α-amylase from<i>Bacillus amyloliquefaciens</i>" @default.
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- W2059411703 doi "https://doi.org/10.1088/0957-4484/22/45/455708" @default.
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