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Overcoming Chronic and Degenerative Diseases with Energy Medicine 1
Published in Aruna Bakhru, Nutrition and Integrative Medicine, 2018
While this might at first seem to be a preposterous idea, there is abundant supporting evidence from the literature of plant physiology. Specifically, red and blue-green algae have intricate light-absorbing structures called phycobilisomes. These “antenna” complexes contain many alpha helical regions, and are described as “light pipes” funneling excitation energy (photons) into the reaction centers of chlorophyll a of photosystem II. Chlorophyll a, in turn, is another membrane protein with five trans-membrane helices (Deisenyhofer Michel and Huber 1985). It is thought that this arrangement enables the algae to survive in weak light environments. The arrangement permits 95% efficiency of energy transfer, as reviewed by Glazer (1985). Moreover, the light sensitive pigment in the human eye, rhodopsin, is also a seven-trans-membrane-helix. Finally, there is evidence for electromagnetic fields acting as first messengers for activating cellular processes without mediation of “second messengers”
Nutritional Composition of the Main Edible Algae
Published in Leonel Pereira, Therapeutic and Nutritional Uses of Algae, 2018
Red algae are rich in phycobiliproteins, i.e., water soluble pigments found in the cytoplasm or in the stroma of the chloroplasts, which are formed by complexes of phycobilins with co-valently bound proteins. Chemically, phycobilins are open-chain tetrapyrrole chromophores bearing A, B, C, and D rings. These chromophores link to the polypeptide chain at conserved positions, either by one cysteinyl thioester linkage through the vinyl substituent on the pyrrole ring A, or occasionally, by two cysteinyl thioester linkages through the vinyl substituent on both A and D pyrrole rings (Cai et al. 2012). The phycobilins are the main component determining the color of the phycobiliproteins. Based on their absorption properties, they can be blue (phycocyanobilin), red (phycoerythrobilin), yellow (phycourobilin), or purple (phycobiliviolin). Molecular pigments are organized in supra-molecular complexes (i.e., phycobilisomes) and they exert a fundamental role in the photosynthetic process of the red algae (Pereira 2009). Phycoerythrin (Fig. 2.5) is the most common phycobiliprotein in many red algae, with levels, on a dry weight basis, of approximately 0.2% for Polysiphonia stricta and Pyropia (as Porphyra) yezoensis, 0.5% for Palmaria palmata and Gracilaria gracilis, and 12% for G. tikvahiae (Romay et al. 2003, Wang 2002, Jespersen et al. 2005, Sekar and Chandramohan 2008, Kim et al. 2013). R-phycoerythrin, together with other phycobiliproteins, have been used for decades as natural colorants in foods (e.g., chewing gum, ice creams, soft drinks, fermented milk products, milk shakes, desserts, jellies, and coated sweet cakes, cosmetic, and pharmaceutical products) (Jespersen et al. 2005, Sekar and Chandramohan 2008). In general, the colors are very stable and tolerate high temperatures, pH changes, and light (Sekar and Chandramohan 2008). Moreover, R-phycoerythrin has specialized applications in analytical techniques, such as flow cytometry, cell sorting, and histo-chemistry (Lorbeer et al. 2013). C-phycocyanin, Rand B-phycoerythrin are currently used in the cosmetic industry for production of lipsticks, eye-liners, and other high value cosmetics (Kim et al. 2013).
Characterization of planktonic and biofilm cells from two filamentous cyanobacteria using a shotgun proteomic approach
Published in Biofouling, 2020
Maria João Leal Romeu, Dany Domínguez-Pérez, Daniela Almeida, João Morais, Alexandre Campos, Vítor Vasconcelos, Filipe J. M. Mergulhão
Allophycocyanin is a protein from the light-harvesting phycobiliprotein family, along with phycocyanin, phycoerythrin and phycoerythrocyanin, which may be found in the phycobilisome core complex (Sonani et al. 2015). Although proteins related to allophycocyanin were found in three of the four biofilm conditions, a protein fragment of phycocyanin beta chain and an additional non-specific phycobilisome protein were identified in both cyanobacterial strains for biofilms formed at 40 s −1. Phycobilisomes are present in cyanobacteria and red algae and are formed by phycobiliproteins and also linker proteins (MacColl 1998). Allophycocyanin is considered an accessory pigment to chlorophyll and exhibits unique absorbance and fluorescence characteristics due to a lack of susceptibility to internal and external fluorescence quenching. Due to these features, allophycocyanin is ideal for highly sensitive studies such as flow cytometry and immunoassays (Manirafasha et al. 2016). Indeed, phycobiliproteins are regularly found in high abundance and they may constitute up to 50% of the total cellular protein of a cyanobacterium (Anderson et al. 2006). Previous proteomic studies with other cyanobacterial strains (Synechocystis PCC 6803) also identified proteins related to this phycobiliprotein family in their plasma membrane (Huang et al. 2002; Pisareva et al. 2007). In another study, which aimed to evaluate proteomic changes after heat shock in Synechocystis PCC 6803, a decreased expression level for phycobilisome was observed (Slabas et al. 2006).