Study of fluorescence quenching of Barley α-amylase

The fluorescence quenching of Barley alpha-amylase by acrylamide and succinimide has been studied in water using steady-state and time-resolved fluorescence techniques. The steady-state fluorescence quenching technique has been performed in three different pHs (i.e., 6,7 and 8) of water. Ground state and excited state binding constants (K-g & K-e) have been calculated. From the calculated binding constants (K-g & K-e) the free energy changes for the ground (Delta G(g)) and excited (Delta G(e)) states have been calculated and are presented in tables. UV and FTIR spectra have also been recorded to prove the binding of Barley alpha-amylase with acrylamide and succinimide. (C) 2011 Elsevier B.V. All rights reserved.