Thermal stabilization of carboxypeptidase A as a function of pH and ionic milieu

Xinhui Li, Beka Solomon

Research output: Contribution to journalArticlepeer-review


In this study we investigated the contribution of pH, phosphate anions and salt concentration to the catalytic and structural thermostability of the carboxypeptidase A (CPA). The concentration of 75-100 mM phosphate as well as neutral pH values were found to be optimal for stabilizing CPA at high temperatures. Although moderate concentrations of sodium chloride had no effect on thermal stability, high concentrations of the salt destabilized the enzyme. The experimental results and theoretical analysis suggested that the main contribution to heat stabilization of CPA is related to intramolecular electrostatic interactions and Arginine and/or Lysine are the putative groups able to bind phosphate and stabilize the enzyme molecule against thermal denaturation.

Original languageEnglish
Pages (from-to)601-611
Number of pages11
JournalBiochemistry and Molecular Biology International
Issue number3
StatePublished - Oct 1997


  • Carboxypeptidase A
  • Electrostatic interactions
  • Microenvironmental effects
  • Phosphate anions
  • Thermostabilization


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