Structural and dynamical features contributing to thermostability in α-amylases


In recent years an increasing number of studies on thermophilic and hyperthermophilic proteins aiming to elucidate determinants of protein thermostability have yielded valuable insights about the relevant mechanisms. In particular, comparison of homologous enzymes with different thermostabilities (isolated from psychrophilic, mesophilic, thermophilic and hyperthermophilic organsims) offers a unique opportunity to determine the strategies of thermal adaptation. In this respect, the medium-sized amylolytic enzyme α-amylase is a well-established representative. Various studies on α-amylases with very different thermostabilities (melting temperature Tm = 40–110°C) report structural and dynamical features as well as thermodynamical properties which are supposed to play key roles in thermal adaptation. Here, results from selected homologous α-amylases are presented and discussed with respect to some new and recently proposed strategies to achieve thermostability.

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Correspondence to J. Fitter.

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Received 28 February 2005; received after revision 29 April 2005; accepted 19 May 2005

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Fitter, J. Structural and dynamical features contributing to thermostability in α-amylases. Cell. Mol. Life Sci. 62, 1925–1937 (2005).

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Key words.

  • Protein stability
  • protein unfolding
  • protein dynamics
  • thermal adaptation
  • unfolded states
  • conformational entropy