title: Studies on kinetic parameters and stability of aminoacylase in non-conventional media.
abstract: 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.
authors.affiliation: Department of Chemistry and Biochemistry, University for Horticulture and Food Industry, Budapest, Hungary.
authors.forename: L
authors.initials: L
authors.lastname: Boross
authors.forename: J
authors.initials: J
authors.lastname: Kosáry
authors.forename: E
authors.initials: E
authors.lastname: Stefanovits-Bányai
authors.forename: C
authors.initials: C
authors.lastname: Sisak
authors.forename: B
authors.initials: B
authors.lastname: Szajáni
mesh_terms: 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
chemical_list: D004146:Dioxanes; D012997:Solvents; D004126:Dimethylformamide; D000581:Amidohydrolases; C019672:aminoacylase I; C025223:1,4-dioxane