甘藷のPhosphorylase

概要

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Sweet potato phosphorylase was purified by the repeated ammonium sulfate precipitation method. Various properties were examined by using this purified enzyme preparation. 1. The dissociation constant between the enzyme and the substrate (the Michaelis constant) was found tobe 2.5×10-3 M glucose-1-phosphate. 2. This purified phosphorylase required added activator for the synthesis of starch from glucose-1-phosphate. 3. Q10 of this enzymatic reaction between 17_??_42°C was about 2, with apparent energy of activation of about 13, 000 cal. 4. Optimum pH of this enzyme was about 5.8, but no significant differences in the enzymatic activities were encountered within pH range of 5.6 - 6.8. 5. Equilibrium of this reaction .was obtained when the value, free P/(free P+esterP), reached 85_??_89%. The equilibrium constant of this reaction, K=5.7-8.0, and the change in the free energy, -ΔF=1, 100_??_1, 400cal. were calculated from the above data.
社団法人日本農芸化学会の論文