Skip to main content


Fig. 3 | Microbial Cell Factories

Fig. 3

From: Enhancement of the catalytic activity of Isopentenyl diphosphate isomerase (IDI) from Saccharomyces cerevisiae through random and site-directed mutagenesis

Fig. 3

Effect of pH on the activity (a) and stability (b) of IDI (L141H/Y195F/W256C) and IDI. a The optimum pH was 7.5 measured at 25 °C. The mutations did not affect the optimal pH for IDI activity, but affect IDI activity for the optimal pH. b The general trends suggested that IDI (L141H/Y195F/W256C) had better pH stability propertied compared to wild-type IDI

Back to article page