A comparative study of the conformational stabilities of trypsin and α-chymotrypsin

Mária L. Simon, Kinga László, Márta Kotormán, Béla Szajáni

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19 Citations (Scopus)


A comparative study was performed on the conformational stabilities of trypsin and α-chymotrypsin. At 45°C, trypsin was most stable at pH 3, while the highest stability of α-chymotrypsin was observed at pH 5. With both ester and amide substrates, trypsin displayed activation at pH 3. In the case of α-chymotrypsin, activation was detected at pH 5 only with the amide substrate. The time curves of heat inactivation were complex. For both enzymes, autolysis proceeded with the highest velocity at pH 8. The results obtained on α-chymotrypsin suggested consecutive reactions: the first step, heat denaturation of the protein, is followed by digestion of the damaged molecules.

Original languageEnglish
Pages (from-to)43-49
Number of pages7
JournalActa Biologica Szegediensis
Issue number1-4
Publication statusPublished - Dec 1 2001


  • Autolysis
  • Conformational stability
  • Trypsin
  • pH effect
  • α-chymotrypsin

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)

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