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

Mária L. Simon, Kinga László, M. Kotormán, B. Szajáni

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

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
Volume45
Issue number1-4
Publication statusPublished - 2001

Fingerprint

Chymotrypsin
chymotrypsin
trypsin
Amides
Trypsin
Chemical activation
amides
Denaturation
Substrates
Hot Temperature
Esters
Protein Denaturation
Autolysis
autolysis
heat inactivation
Molecules
Enzymes
Digestion
digestion
esters

Keywords

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

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Cell Biology
  • Applied Microbiology and Biotechnology
  • Neuroscience(all)

Cite this

A comparative study of the conformational stabilities of trypsin and α-chymotrypsin. / Simon, Mária L.; László, Kinga; Kotormán, M.; Szajáni, B.

In: Acta Biologica Szegediensis, Vol. 45, No. 1-4, 2001, p. 43-49.

Research output: Contribution to journalArticle

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