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.
journal_name
J Biotechnoljournal_title
Journal of biotechnologyauthors
Boross L,Kosáry J,Stefanovits-Bányai E,Sisak C,Szajáni Bdoi
10.1016/s0168-1656(98)00158-8subject
Has Abstractpub_date
1998-11-18 00:00:00pages
69-73issue
1eissn
0168-1656issn
1873-4863pii
S0168-1656(98)00158-8journal_volume
66pub_type
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