Functional expression of an orchid fragrance gene in Lactococcus lactis

Int J Mol Sci. 2012;13(2):1582-1597. doi: 10.3390/ijms13021582. Epub 2012 Feb 2.

Abstract

Vanda Mimi Palmer (VMP), an orchid hybrid of Vanda tesselata and Vanda Tan Chay Yan is a highly scented tropical orchid which blooms all year round. Previous studies revealed that VMP produces a variety of isoprenoid volatiles during daylight. Isoprenoids are well known to contribute significantly to the scent of most fragrant plants. They are a large group of secondary metabolites which may possess valuable characteristics such as flavor, fragrance and toxicity and are produced via two pathways, the mevalonate (MVA) pathway or/and the 2-C-methyl-D-erythritol-4-phosphate (MEP) pathway. In this study, a sesquiterpene synthase gene denoted VMPSTS, previously isolated from a floral cDNA library of VMP was cloned and expressed in Lactococcus lactis to characterize the functionality of the protein. L. lactis, a food grade bacterium which utilizes the mevalonate pathway for isoprenoid production was found to be a suitable host for the characterization of plant terpene synthases. Through recombinant expression of VMPSTS, it was revealed that VMPSTS produced multiple sesquiterpenes and germacrene D dominates its profile.

Keywords: Lactococcus lactis; Vanda Mimi Palmer; fragrance; isoprenoids; orchid; sesquiterpene synthase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alkyl and Aryl Transferases / biosynthesis*
  • Alkyl and Aryl Transferases / genetics
  • Genes, Plant*
  • Lactococcus lactis / genetics*
  • Magnoliopsida / enzymology
  • Magnoliopsida / genetics*
  • Oils, Volatile / metabolism*
  • Plant Proteins / biosynthesis*
  • Plant Proteins / genetics
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / genetics
  • Terpenes / metabolism

Substances

  • Oils, Volatile
  • Plant Proteins
  • Recombinant Proteins
  • Terpenes
  • Alkyl and Aryl Transferases
  • terpene synthase