Stability of hydrolytic enzymes in water-organic solvent systems

L. M. Simon, K. László, A. Vértesi, K. Bagi, B. Szajáni

Research output: Contribution to journalArticle

57 Citations (Scopus)

Abstract

The effects of organic solvents on the stabilities of bovine pancreas trypsin, chymotrypsin, carboxypeptidase A and porcine pancreas lipase were studied. Water-miscible solvents (ethanol, acetonitrile, 1,4-dioxane and dimethyl sulfoxide) and water-immiscible solvents (ethyl acetate and toluene) were used in 100 mM phosphate buffer (pH 7.0) or 100 mM Tris/HCl buffer (pH 7.0) in concentrations of 20-80% (v/v). All hydrolytic enzymes studied were inactivated by mixtures containing dimethyl sulfoxide at higher concentrations. Trypsin and carboxypeptidase A resisted solvent mixtures containing acetonitrile, 1,4-dioxane and ethanol. They preserved more than 80% of their starting activities during 20-min incubations. The activities of lipase and chymotrypsin decreased with increasing concentration of water- miscible polar organic solvents, but at higher concentrations (80%) 70-90% of the activity remained. In mixtures with water-immiscible solvents, the decrease in activity of carboxypeptidase A was pronounced. Trypsin and chymotrypsin underwent practically no loss in activity in the presence of toluene or ethyl acetate. In respect of stability, the polar solvent proved to be more favorable for lipase. These results suggest that the conformational stabilities of hydrolytic enzymes are highly dependent on the solvent-protein interactions and the enzyme structure.

Original languageEnglish
Pages (from-to)41-45
Number of pages5
JournalJournal of Molecular Catalysis B: Enzymatic
Volume4
Issue number1-2
DOIs
Publication statusPublished - Jan 2 1998

Fingerprint

Enzyme Stability
Organic solvents
Enzymes
Carboxypeptidases A
Water
Lipases
Lipase
Dimethyl sulfoxide
Toluene
Dimethyl Sulfoxide
Acetonitrile
Buffers
Ethanol
Pancreas
Chymotrypsin
Trypsin
Tromethamine
Phosphates
Proteins
Swine

Keywords

  • Carboxypeptidase A
  • Chymotrypsin
  • Conformational stability
  • Lipase
  • Organic solvent effects
  • Trypsin

ASJC Scopus subject areas

  • Biochemistry
  • Catalysis
  • Process Chemistry and Technology

Cite this

Stability of hydrolytic enzymes in water-organic solvent systems. / Simon, L. M.; László, K.; Vértesi, A.; Bagi, K.; Szajáni, B.

In: Journal of Molecular Catalysis B: Enzymatic, Vol. 4, No. 1-2, 02.01.1998, p. 41-45.

Research output: Contribution to journalArticle

Simon, L. M. ; László, K. ; Vértesi, A. ; Bagi, K. ; Szajáni, B. / Stability of hydrolytic enzymes in water-organic solvent systems. In: Journal of Molecular Catalysis B: Enzymatic. 1998 ; Vol. 4, No. 1-2. pp. 41-45.
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