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

ABSTRACT:

Background

Lycopene is a terpenoid pigment that has diverse applications in the food and medicine industries. A prospective approach for lycopene production is by metabolic engineering in microbial hosts, such as Escherichia coli. Isopentenyl diphosphate isomerase (IDI, E.C. 5.3.3.2) is one of the rate-limiting enzymes in the lycopene biosynthetic pathway and one major target during metabolic engineering. The properties of IDIs differ depending on the sources, but under physiological conditions, IDIs are limited by low enzyme activity, short half-life and weak substrate affinity. Therefore, it is important to prepare an excellent IDI by protein engineering.

Results

Directed evolution strategy (error-prone PCR) was utilized to optimize the activity of Saccharomyces cerevisiae

SUBMITTER: Chen H 

PROVIDER: S-EPMC5925831 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature