Heterologous reconstitute of Spirulina platensis (Cyanobacteria) polyunsaturated fatty acid biosynthesis pathway in yeast, Saccharomyces cerevisiae
2006
Prommeenate, P. | Hongsthong, A. | Kurdrit, P. | Cheevadhanarak, S. | Tanticharoen, M., King Mongkut's Univ. of Technology, Thonburi, Bangkhuntein, Bangkok 10150 (Thailand). National Center for Genetic Engineering and Biotechnology
The reconstitution of fatty acid biosynthesis in Spirulina platensis has been studied in a heterologous host, Saccharomyces cerevisiae. The Spirulina-delta sup 6 and delta sup 12-desaturase genes were co-transformed and heterologously expressed in yeast, S. cerevisiae. Co-expressiom of both desaturases resulted in accumulation of polyunsaturated fatty acids (PUFAs), revealing the functional activity of Spirulina-delta sup 6 and delta sup 12 desaturase enzymes in the yeast cells. The desaturation reactions in cyanobacteria have been reported to be involved with ferredoxin as an electron donor, whereas the acyl-lipid desaturase reaction in plant and the acyl-CoA desaturase of animal and fungi used cytochrome b sub b5. However, extensive studies on recombinant protein of Spirulina delta sup 6 desaturase revealed the complementary role of cytochrome b sub5 in the desaturation process carried out by Spirulina delta sup 6 desaturase. Therefore, in the present study, the free form of cytochrome b sub 5 domain was co-expressed with Spirulina delta sup 6 and delta sup 12 desaturase into the S. cerevisiae system. The results not only support the complementary role of cytochrome b sub 5 in PUFAs production by Spirulina-desaturase in the yeast cell but also show the enhancement of PUFA production in vivo. The data indicates that the amount of an immediate cofactor in the cells is critical for PUFA production.
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