FT-IR STUDIES OF α-ASPARTYL DIPEPTIDASE AND ITS EVOLUTIONAL ENZYME
α-天门冬氨酰二肽酶及其进化酶的FT-IR 研究

Under double screen pressure of specific activity and thermo stablity, an evolved α-aspartyl dipeptidase, with 47 folds higher activity than its wild type ancestor, was obtained. By using FT-IR, the secondary structure of α-aspartyl dipeptidase and its evolutional enzyme were studied. It is found that α-helix structure is 31%,β-sheet content is 26.8% while turn and random coil component are 42.2% in the evolutional type of α-aspartyl dipeptidase .In the wild type enzyme, α-helix structure is 33%, β-sheet content is 28.5% and turn and random coil are 38.5%.These structure changes lead to arise the flexibility of evolutional type and adaptability to substrate.