Correction: Directed evolution of mevalonate kinase in Escherichia coli by random mutagenesis for improved lycopene.

[This corrects the article DOI: 10.1039/C8RA01783B.]. This journal is © The Royal Society of Chemistry.

The authors wish to draw the readers’ attention to their closely related paper, published in Microbial Cell Factories,[1] which should have been cited in this RSC Advances paper.

The authors regret that there is unattributed overlap in text between this RSC Advances paper and ref. 1. The authors confirm that new data has been reported in this RSC Advances article.

Two different rate-limiting enzymes in the lycopene synthetic pathway were studied using the same methods, mevalonate kinase (MK) in this paper and isopentenyl diphosphate isomerase (IDI) in ref. 1. In the RSC Advances paper, a directed evolution strategy was used to optimize the activity of MK to enhance the tolerance for farnesyldiphosphate (FPP) and geranylgeranyldiphosphate (GGPP), to enhance the affinity of mevalonate and MK, and to improve lycopene production. The catalytic mechanisms of both enzymes are very different; however improving their activities can improve lycopene production.

The Royal Society of Chemistry apologises for these errors and any consequent inconvenience to authors and readers.