Functional Expression of an Orchid Fragrance Gene in Lactococcus lactis

International Journal of Molecular Sciences

Adelene Ai Lian Song²  Janna O. Abdullah¹  Mohd Puad Abdullah²  Norazizah Shafee¹ 

[1] Department of Microbiology, Faculty of Biotechnology and Biomolecular Sciences, University Putra Malaysia, 43400, UPM Serdang, Malaysia; E-Mails:;Department of Cell and Molecular Biology, Faculty of Biotechnology and Biomolecular Sciences, University Putra Malaysia, 43400, UPM Serdang Selangor, Malaysia; E-Mails:

关键词: Vanda Mimi Palmer;    Lactococcus lactis;    isoprenoids;    sesquiterpene synthase;    orchid;    fragrance;   

DOI  :  10.3390/ijms13021582

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2012 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland.