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Fig. 4 | Microbial Cell Factories

Fig. 4

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

Fig. 4

Effect of temperature on the activity (a) and stability (b) of IDI (L141H/Y195F/W256C) and IDI. a The optimal temperature was 35 °C, and that mutations did not affect the optimal temperature for IDI activity. b The thermal stabilities of both IDIs continuously decreased at temperature above 35 °C, while the thermal stability of wild-type IDI decreased more significantly than IDI (L141H/Y195F/W256C)

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Microbial Cell Factories

ISSN: 1475-2859

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