Plant made industrial compounds (PMIs)
Plant molecular farming is starting to become a viable new industry. This group includes hydrolases, encompassing glycosidases and proteases, milk proteins ß-casein, lactoferrin and lysozyme, protein polymers tissue replacement (Ma et al., 2003). Expression of thioredoxin in foods such as cereal grains would increase the digestibility of proteins and thereby reduce their allergenicity (Thomas et al., 2002). Human collagen can be produced in transgenic tobacco plants and that the protein is spontaneously processed and assembled into its typical triple-helical conformation (Ma et al., 2003). The production of chicken egg white avidin in transgenic corn using an avidin gene with codonoptimization was achieved (Hood et al., 1997). The endoplasmic reticulum of transgenic tobacco and vacuole of potato tubers expressed recombinant dragline silk protein up to 2% of TSP (Scheller et al., 2001). Several other products have been produced in plants which include streptavidin, acetyl cholinesterase, hirudin, protein C, human β casein, vegetable oils, collagen, gamma-amino butyric acid, β-glucuronidase, cyclodextrins, enzymes like phytases, xylanases, amylase, laccase, glucanases and trans glutaminases (Akama et al., 2009; Boehm, 2007; Cahoon et al., 2007)
For efficient production of recombinant products, the selection of the host plant plays an important role (Sharma and Sharma, 2009). Apart from this, the life cycle of the host, biomass yield, containment, scale-up costs, the form of recombinant protein, ease of downstream processing are the deciding factors. The site of protein localization in the plant cell is another important criterion which decides the correct protein folding and its yield. Various plant organs (leaves, roots, seeds) and plant cell compartments (endoplasmic reticulum, vacuole, chloroplast, oil bodies) are being tested as sites for recombinant protein accumulation (Goldstein and Thomas, 2004).
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