A Rapid Method for Secondary-Structure Analysis of the Inulinases of Different Microbial Producers

Abstract

Computer simulation of secondary structures (calculation of the ratio of α-helices, β-sheets and disordered regions) is a perspective tool needed at the initial stages of the studies of structural and functional features of inulinases, since it enables one to estimate the fluctuation ranges of tested indicators. However, the data from computations should be verified by a number of biophysical and biochemical experimental data, in particular, by experiments using IR-spectroscopy. In the present work, the difference between the experimental and computational data was 3–4% for inulinase from Aspergillus awamori and 12–18% for the enzyme from Kluyveromyces marxianus. Consequently, the analysis of secondary structures of enzymes is applicable for making rapid predictions of the fluctuation ranges of physical−chemical and kinetic characteristics of protein molecules, as well as for rapid evaluation of their dynamic state.