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Bacteriocin Release Protein-Mediated Secretory Expression of Recombinant Chalcone Synthase in Escherichia coli

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Abstract

Flavonoids are secondary metabolites synthesized by plants shown to exhibit health benefits such as anti-inflammatory, antioxidant, and anti-tumor effects. Thus, due to the importance of this compound, several enzymes involved in the flavonoid pathway have been cloned and characterized in Escherichia coli. However, the formation of inclusion bodies has become a major disadvantage of this approach. As an alternative, chalcone synthase from Physcomitrella patens was secreted into the medium using a bacteriocin release protein expression vector. Secretion of P. patens chalcone synthase into the culture media was achieved by co-expression with a psW1 plasmid encoding bacteriocin release protein in E. coli Tuner (DE3) plysS. The optimized conditions, which include the incubation of cells for 20 h with 40 ng/ml mitomycin C at OD600 induction time of 0.5 was found to be the best condition for chalcone synthase secretion.

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Acknowledgments

This research was supported by the Malaysia Genome Institute (07-05-MGI-GMB01).

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Authors and Affiliations

  1. Faculty of Biotechnology and Biomolecular Sciences, Enzyme and Microbial Technology Research Group, Universiti Putra Malaysia, Serdang, Malaysia

    Iffah Izzati Zakaria, Raja Noor Zaliha Raja Abdul Rahman & Abu Bakar Salleh

  2. Faculty of Science, Universiti Putra Malaysia, 43400 UPM, Serdang, Malaysia

    Iffah Izzati Zakaria & Mahiran Basri

Authors
  1. Iffah Izzati Zakaria
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  2. Raja Noor Zaliha Raja Abdul Rahman
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  3. Abu Bakar Salleh
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  4. Mahiran Basri
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Correspondence to Raja Noor Zaliha Raja Abdul Rahman.

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Zakaria, I.I., Rahman, R.N.Z.R.A., Salleh, A.B. et al. Bacteriocin Release Protein-Mediated Secretory Expression of Recombinant Chalcone Synthase in Escherichia coli . Appl Biochem Biotechnol 165, 737–747 (2011). https://doi.org/10.1007/s12010-011-9292-1

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  • DOI: https://doi.org/10.1007/s12010-011-9292-1

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