Biochemical and Structural Characterization of Amy1: An Alpha-Amylase from Cryptococcus flavus Expressed in Saccharomyces cerevisiae
Figure 4
Far-UV circular dichroism analyses. Residual molar ellipticity [θ] was measured from 200 to 260 nm at 25°C or temperature arising from 25 to 95°C. (a) The distinct spectra of wild-type (Amy1w) and recombinant (Amy1) amylase are shown, indicating that they had different amount of secondary structure (see Section 3). (b) Effect of temperature on secondary structure of Amy1. Changes in molar ellipticity at 222 and 200 nm are shown as a function of temperature. (c) Effect of pH on secondary structure of Amy1. Note the slight differences of CD spectra at pH 7.0, 3.0, and 5.5 and similarity of CD spectra at pH 4.0 and 8.0. (d) Effect of temperature on secondary structure of Amy1w. Changes in molar ellipticity at 222 and 206 nm are shown as a function of temperature.
