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RETRACTED ARTICLE: Enhancement of the catalytic activity of ferulic acid decarboxylase from Enterobacter sp. Px6-4 through random and site-directed mutagenesis

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This article was retracted on 07 October 2016

Abstract

The enzyme ferulic acid decarboxylase (FADase) from Enterobacter sp. Px6-4 catalyzes the decarboxylation reaction of lignin monomers and phenolic compounds such as p-coumaric acid, caffeic acid, and ferulic acid into their corresponding 4-vinyl derivatives, that is, 4-vinylphenol, 4-vinylcatechol, and 4-vinylguaiacol, respectively. Among various ferulic acid decarboxylase enzymes, we chose the FADase from Enterobacter sp. Px6-4, whose crystal structure is known, and produced mutants to enhance its catalytic activity by random and site-directed mutagenesis. After three rounds of sequential mutations, FADase(F95L/D112N/V151I) showed approximately 34-fold higher catalytic activity than wild-type for the production of 4-vinylguaiacol from ferulic acid. Docking analyses suggested that the increased activity of FADase(F95L/D112N/V151I) could be due to formation of compact active site compared with that of the wild-type FADase. Considering the amount of phenolic compounds such as lignin monomers in the biomass components, successfully bioengineered FADase(F95L/D112N/V151I) from Enterobacter sp. Px6-4 could provide an ecofriendly biocatalytic tool for producing diverse styrene derivatives from biomass.

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Acknowledgments

This work was supported by a grant from National Research Foundation grant (NRF:2010-0029224) of the Ministry of Education Science and Technology, Republic of Korea.

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The authors declare that they have no competing interests.

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The authors followed principles of ethical and professional conduct in this research and in the preparation of this manuscript.

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Correspondence to Hor-Gil Hur.

Additional information

This article has been retracted at the request of the authors.

The corresponding author, Hor-Gil Hur, reported to the Editor-in-Chief that the authors of this manuscript have raised concerns related to the accuracy of the data presented in this article. The authors determined that the enzyme activity data from the experiments performed by the authors are not consistent when tested repeatedly and the mutant does not show 34 fold higher catalytic activity compared to wild type which was the major claim in this manuscript. This is the major reason for the retraction of the manuscript. However, the authors did not find out the exact reason why it does not show reproducible data. It may be miscalculation or wrong interpretation of the data.

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Lee, H., Park, J., Jung, C. et al. RETRACTED ARTICLE: Enhancement of the catalytic activity of ferulic acid decarboxylase from Enterobacter sp. Px6-4 through random and site-directed mutagenesis. Appl Microbiol Biotechnol 99, 9473–9481 (2015). https://doi.org/10.1007/s00253-015-6717-8

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  • DOI: https://doi.org/10.1007/s00253-015-6717-8

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