|
This glucose isomerizing enzyme, which Actinomyces sp. (strain, K-17) produced, was inhibited by citrate, oxalate, ethylene diamine tetraacetic acid and cysteine on the enzyme reaction. This enzyme isomerized xylose to ketose as well as glucose. The Michaelis constant of this enzyme was 7.2×10^(-1)M. on D-glucose. The enzyme activity of intact cells which were harvested in the none xylose containing medium was very weak. If these intact cells of low activity were treated in the buffered xylose solution, its activity was considerably increased. After fifteen hours at 32℃. on xylose treatment, the enzyme activity was increased to equilibrium and the treating condition was proper at neutral pH and in aerobic state. The adequate concentration of xylose on the treatment was about 0.5 percent.
|