Studies on kinetic parameters and stability of aminoacylase in non-conventional media

• Published in: Journal of biotechnology Vol. 66; no. 1; pp. 69 - 73
• Main Authors: Boross, L, Kosáry, J, Stefanovits-Bányai, É, Sisak, C, Szajáni, B
• Format: Journal Article Conference Proceeding
• Language: English
• Published: Lausanne Elsevier B.V 18.11.1998; Amsterdam Elsevier; New York, NY
• Subjects: Amidohydrolases - chemistry; Amidohydrolases - drug effects; Amidohydrolases - metabolism; Aminoacylase; Binary mixtures; Bioconversions. Hemisynthesis; Biological and medical sciences; Biotechnology; Catalysis; Catalyst activity; Catalyst deactivation; Conformations; Dimethylformamide - chemistry; Dimethylformamide - pharmacology; Dioxane; Dioxanes - chemistry; Dioxanes - pharmacology; Enzyme inhibition; Enzyme Stability; Fundamental and applied biological sciences. Psychology; Kinetic parameters; Kinetics; Methods. Procedures. Technologies; N, N-dimethylformamide; Nitrogen compounds; Non-conventional media; Solvents; Stability; Dioxane; Stability; Kinetic parameters; Aminoacylase; N, N-dimethylformamide; Non-conventional media; Enzyme; Environmental factor; Kidney; Pig; Organic solvent; Vertebrata; Mammalia; Enzymatic activity; Hydrolases; Artiodactyla; Kinetic parameter; Ungulata; Comparative study
• ISSN: 0168-1656; 1873-4863
• DOI: 10.1016/S0168-1656(98)00158-8

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 ( t 1/2 39 min), while in the case of 20% DMF the enzyme practically lost its starting activity during 50 min incubation ( t 1/2 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 V max value decreased practically to zero in the same concentration range.