| Abstrakt: |
The effect of cations and anions on the activity of Achromobacter sp. 7a α-amylase was studied. It is shown that tested enzyme is stable to most of anions, however sensitive to a number of cations. The most significant inhibitory effects on the activity of Achromobacter sp. 7a α-amylase exerted Hg2+, Al3+, Fe3+, Cu2+ and Ag+ ions. Decline of activity Achromobacter sp. 7a α-amylase in the presence of EDTA and EGTA indicated on the presence within its structure of metal ions. An important role in the functioning of this enzyme play a carboxyl and sulfhydryl groups as evidenced by its inhibition of 1-[3-(dimethylamino)propyl]-3-ethylcarbodiimide methiodide and p-chloromercuribenzoate respectively. α-Amylase Achromobacter sp. 7a does not contain histidine imidazole group in the active center, unlike most studied glycosidases. The tested enzyme showed high stability in the presence of Tween-20, urea, peroxide of hydrogen, making it competitive with previously described α-amylases. |
