원문정보
초록
영어
In our previous study, we reported that the 30K protein originating from silkworm, Bombyx mori, inhibited apoptosis in mammalian cells. In this study, a novel effect of 30K protein was investigated; the enzyme-stabilizing effect. When the Alkaline Phosphatase (AP) was diluted in deionized water and incubated at 37℃, the enzyme was deactivated with respect to time, then the activity decreased to 30% from the initial activity for 2 h. However, the AP deactivation was
inhibited significantly in the case of 30K protein addition. When the 8 μg/ml of 30K protein was added to enzyme mixture, the AP activity was sustained to 90% from the initial activity for 2 h incubation period. The similar result was obtained in the case of Horseradish Peroxidase (HRP). According to the first-order enzyme deactivation kinetics, we have estimated the deactivation constant, Kd. In the case of AP, Kd value was decreased less than 20% compared to control
when the 8μg/ml of 30K protein was added. The enzyme-stabilizing effect of 30K protein was also observed in various temperatures and buffer systems. We expect that the use of 30K protein would provide a new strategy for improvement of the stability in various industrial
enzyme reactions.