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Functional Expression of an Orchid Fragrance Gene in Lactococcus lactis

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Author(s): Adelene Lian Ai Song | Janna O. Abdullah | Puad Abdullah | Norazizah Shafee | Raha A. Rahim

Journal: International Journal of Molecular Sciences
ISSN 1422-0067

Volume: 13;
Issue: 2;
Start page: 1582;
Date: 2012;
Original page

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

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.
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