Macromolecular Crowding Enhances Catalytic Efficiency and Stability of α-Amylase
Figure 4
Intrinsic fluorescence of α-amylase in the presence of cosolvents. Figures 4(a), 4(b), 4(c), and 4(d) represent the activity profiles of the enzyme in the presence of glycerol, sorbitol, sucrose, and trehalose, respectively. The curves are represented as (a) the enzyme in buffer, (b) in 20%, and (c) in 40% of respective cosolvents.
