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The paper presents the impact of variable environment acidity and low temperature on the stability of biosensor receptor layer component BSA (Bovine Serum Albumin). With the use of UV/Vis spectrophotometer, absorption spectra in range (250-300nm) was taken to study conformational changes of the protein with time after exposition to different factors. The results showed an increase in absorption, associated with the conformational changes of BSA with time. A significant decrease in the absorption intensity was note...

The paper presents the impact of variable environment acidity and low temperature on the stability of biosensor receptor layer component BSA (Bovine Serum Albumin). With the use of UV/Vis spectrophotometer, absorption spectra in range (250-300nm) was taken to study conformational changes of the protein with time after exposition to different factors. The results showed an increase in absorption, associated with the conformational changes of BSA with time. A significant decrease in the absorption intensity was note...