Studies on kinetic parameters and stability of aminoacylase in non-conventional media.
Catalytic properties and conformational stability of aminoacylase (N-acylamino acid amidohydrolase, EC 3.5.1.14) were studied in water-N,N-dimethylformamide (DMF) and water-dioxane solvent mixtures. Beside the prompt inhibition the solvents caused further inactivation during incubations. In the presence of 5% DMF content the inactivation proceeds with a well-measurable rate (t1/2 39 min), while in the case of 20% DMF the enzyme practically lost its starting activity during 50 min incubation (t1/2 13 min). The K(m) value of the enzyme increased about three times with increasing DMF concentrations up to about 2.6 M DMF, while the Vmax value decreased practically to zero in the same concentration range.
Boross
L
L
Department of Chemistry and Biochemistry, University for Horticulture and Food Industry, Budapest, Hungary.
Kosáry
J
J
Stefanovits-Bányai
E
E
Sisak
C
C
Szajáni
B
B
D000581:Amidohydrolases / Q000737:chemistry* / Q000187:drug effects / Q000378:metabolism*; D004126:Dimethylformamide / Q000737:chemistry / Q000494:pharmacology; D004146:Dioxanes / Q000737:chemistry / Q000494:pharmacology; D004795:Enzyme Stability; D007700:Kinetics; D012997:Solvents
D004146:Dioxanes; D012997:Solvents; D004126:Dimethylformamide; D000581:Amidohydrolases; C019672:aminoacylase I; C025223:1,4-dioxane