The life cycle of Spirulina (Figure 5.2) in laboratory culture is rather simple. A mature trichome is broken into several pieces through the formation of specialized cells, necridia, that undergo lysis, giving rise to biconcave separation disks. The fragmentation of the trichome at the necridia produces gliding, short (two to four cells) chains of cells, and the hormogonia, which move away from the parental filament to give rise to a new trichome. The cells in the hormogonium lose the attached portions of the necridial cells, becoming rounded at the distal ends with little or no thickening of the walls. During this process, the cytoplasm appears less granulated and the cells assume a pale blue-green color.7
Like most cyanobacteria, Spirulina is an obligate photoautotroph and cannot grow in the dark in media containing organic sources of carbon. The phycocyanin, biliproteins involved in the light-harvesting reactions, have been resolved by gel electrophoresis in S. platensis and S. maxima and isolated from the former. Both
c-phycocyanin and allophycocyanin appear to be oligomeric complexes composed of at least two different subunits that may be resolved by electrophoresis under denaturing conditions.8,9 Cytochrome C554, a cytochrome with high redox potential that links photosystems I and II, has been purified from S. platensis and S. maxima.10 Ferredoxin, one of the electron carriers of photosynthesis, was purified from S. maxima and sequenced from S. maxima and S. platensis.11
Spirulina has high protein content 45% of the dry weight in the samples and 62% in laboratory-grown S. platensis. More recent analysis confirmed that protein represents more than 60% and, in certain samples, even 70% of the dry weight. The protein content of Spirulina appears to be high when compared with that of unicellular algae and other cyanobacteria.
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