• Journal of the Korean Society of Food Science and Nutrition
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• v.20 no.2
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• pp.179-186
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• 1991

The nutritional requirement and cultural condition such as carbon and nitrogen sources, cultural temperature, initial pH, cultural time and aeration for the production of endocellular cytosine deaminase from Aspergillus fumigatus IFO 5840 were investigated. The cultural broth giving maximum cytosine deaminase yield was found to consist of 2% glucose as a carbon source and 1% yeast extract and 0.1% peptone as a nitrogen source. Optimal initial pH of the culture broth was pH 8.5 and the enzyme production in the cell usually reached a maximum after 28 hours of cultivation in the 500ml shaking flask containing 100ml broth at $30^{\circ}C$. The endoenzyme production of the used strain was inhibited by inorganic nitrogen, but activated by orgainc nitrogen, yeast extract.

• Journal of the Korean Society of Food Science and Nutrition
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• v.21 no.3
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• pp.279-285
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• 1992

Cytidine deaminase (EC 3.5.4.5) from Aspergillus fumigatus IFO 5840, which was the first cytidine deaminase to be found in a mold, was fractionated with ammonium sulfate (35-60%). When the enzyme solution in 0.25M of Tris-HCI buffer (pH 7.2) was preincubated at $37^{\circ}C$ for 25min, the enzyme activity was reached to maximum state. The optimum pH and temperature for the enzyme activity were found to be 6.8 to 7.2 and near $37^{\circ}C$, respectively. The enzyme was stable in a pH 7.2 to 9.0, and was generally stable at 4$0^{\circ}C$, but after treating at 6$0^{\circ}C$ for 20min at the optimal pH, 17% of the enzyme activity was inactivated, and disappeared completely by treating at 1$0^{\circ}C$ for 25min. Activation energy (Ea) of fungal cytidine deaminase was calculated as 14.190 Kcal /mol by the Arrhenius plot, and temperate coeffient ($Q_{10}$ ) of the enzyme was calculated as 2.163.

• The Korean Journal of Food And Nutrition
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• v.10 no.1
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• pp.53-59
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• 1997

In this study investigated the effect of cytosine deaminase activity from Aspergillus fumigatus IFO 5840 by cytosine analogues. The results were as follows. The enzyme was strongly inibited by 2-thiouracil, 2-thiocytosine, 6-azacytosine and 2-mercaptopyrimidine. The half inhibitory concentration(HIC) of 2-thiocytosine and 6-azacytosine on cytosine deaminase was 0.80mM and 1.15mM, respectively. The enzyme was inhibited at a certain level by addition of 2-thiocytosine immediately, but was maintained to some extend under the inhibited state by 6-azacytosine in proportion to reaction time. Regardless of kinds of substrate such as cytosine and 5-fluorocytosine, 2-thiocytosine and 6-azacytosine showed action as inhibitors, 2-thiocytosine inhibited cytosine deaminase activity about twice as strong as 6-azacytosine. The enzyme, when cytosine was used as a substrate, was revealed the pattern of competitive inhibition by 2-thiocytosine and 6-azacytosine, The ki value for these compounds was 4.5$\times$10-4M and 1.756$\times$10-3M, respectively. At this point, the Hill coefficient for cytosine, 2-thiocytosine and 6-azacytosine was 1.80, 1.81 and 2.45, respectively.