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Phycobiliproteins As a Commodity: Trends in Applied Research, Patents and Commercialization

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Phycobiliproteins As a Commodity: Trends in Applied Research, Patents and Commercialization J Appl Phycol (2008) 20:113–136 DOI 10.1007/s10811-007-9188-1 Phycobiliproteins as a commodity: trends in applied research, patents and commercialization Soundarapandian Sekar & Muruganandham Chandramohan Received: 23 March 2007 /Revised and accepted: 25 May 2007 /Published online: 16 August 2007 # Springer Science + Business Media B.V. 2007 Abstract Phycobiliproteins are a group of colored proteins means for improvements in the application and production commonly present in cyanobacteria and red algae possess- of phycobiliproteins. ing a spectrum of applications. They are extensively commercialized for fluorescent applications in clinical and Keywords Colorant . Cyanobacteria . Fluorophore . Patent immunological analysis. They are also used as a colorant, analysis . Phycobiliprotein extraction . Red alga and their therapeutic value has also been categorically demonstrated. However, a comprehensive knowledge and technological base for augmenting their commercial utilities is lacking. Hence, this work is focused towards this Introduction objective by means of analyzing global patents and commercial activities with application oriented research. The phycobiliproteins (PBPs) are antennae-protein pigments Strategic mining of patents was performed from global involved in light harvesting in cyanobacteria (blue-green patent databases resulting in the identification of 297 algae, procaryotic), rhodophytes (red algae, eukaryotic), patents on phycobiliproteins. The majority of the patents cryptomonads (biflagellate unicellular eukaryotic algae) and are from USA, Japan and Europe. Patents are grouped into cyanelles (endosymbiotic plastid-like organelles) (Glazer fluorescent applications, general applications and produc- 1994). In cyanobacteria and red algae, the phycobiliproteins tion aspects of phycobiliproteins and the features of each are organized in supramolecular complexes, called phycobi- group are discussed. Commercial and applied research lisomes (PBSs), which are assembled in regular arrays on the activities are compared in parallel. It revealed that US outer surface of the thylakoid membranes. Phycobiliproteins patents are mostly related to fluorescent applications while are oligomeric proteins, built up from chromophore-bearing Japanese are on the production, purification and application polypeptides belonging to two families (α and β) probably for therapeutic and diagnostic purposes. Fluorescent appli- originating from a common ancestor (Glazer 1989). The cations are well represented in research, patents and colors of phycobiliproteins originate mainly from covalently commercial sectors. Biomedical properties documented in bound prosthetic groups that are open-chain tetrapyrrole research and patents are not ventured commercially. Several chromophores bearing A, B, C and D rings named novel applications are reported only in patents. The paper phycobilins. They are either blue colored phycocyanobilin further pinpoints the plethora of techniques used for cell (PCB), red colored phycoerythrobilin (PEB), the yellow breakage and for extraction and purification of phycobili- colored phycourobilin (PUB), or the purple colored phyco- proteins. The analysis identifies the lacuna and suggests biliviolin(PXB), also named cryptoviolin. These chromo- phores are generally bound to the polypeptide chain at conserved positions either by one cysteinyl thioester linkage through the vinyl substituent on the pyrrole ring A of the * : S. Sekar ( ) M. Chandramohan tetrapyrrole or occasionally by two cysteinyl thioester link- Department of Biotechnology, Bharathidasan University, Tiruchirappalli 620 024, India ages through the vinyl substituent on both A and D pyrrole e-mail: [email protected] rings (Glazer 1985). 114 J Appl Phycol (2008) 20:113–136 In cyanobacteria and red algae, four main classes of than trimers or hexamers, and (5) they contain several phycobiliproteins exist: allophycocyanin (APC, bluish unusual bilins, for example in the cryptophycean biliprotein green), phycocyanin (PC, blue), phycoerythrin (PE, purple), phycocyanin 645, three chemically different bilins such as and phycoerythrocyanin (PEC, orange) having lAmax of Cys-bilin 618, DiCys-bilin 584 and Cys-bilin 584 are 650–655 nm, 615–640 nm, 565–575 nm and 575 nm, present (Becker et al. 1998; Wedemayer et al. 1991). respectively and emit light at 660 nm, 637 nm, 577 nm and Cyanobacterial phycobiliproteins have gained impor- 607 nm, respectively (Bryant et al. 1979). Isolated intact tance in the commercial sector, as they have several appli- phycobilisomes exhibit a fluorescence emission maximum cations. The primary potential of these molecules are as of ∼680 nm (Gantt and Lipschuttz 1973). Light energy is natural dyes but a number of investigations have shown on absorbed mainly by the pheripheral rods, where the shortest their health-promoting properties and broad range of wavelength absorbing phycobiliproteins (PE or PEC) are pharmaceutical applications. Thus, one of the applications located. The light energy absorbed by PE or PEC is of phycocyanin is to use as food pigment replacing current transferred by radiationless dipole induced dipole resonance synthetic pigments. They are used as a colourant in energy transfer to C-phycocyanin and then to allophyco- chewing gum, ice sherberts, popsicles, candies, soft drinks, cyanin (APC) and finally transmitted to PS II (and partially) dairy products and cosmetics like lipstick and eyeliners. In to PS I reaction centers (Suter and Holzwarth 1987). addition, phycobiliproteins are widely used in clinical and The assembly of the phycobilisome is stabilized by a immunological research laboratories (Spolaore et al. 2006). group of polypeptides named ‘linker’ polypeptides (L). They serve as labels for antibodies, receptors and other They induce a face-to-face aggregation of phycoerythrin or biological molecules in a fluorescence-activated cell sorter, phycoerythrocyanin and phycocyanin trimers. They addi- and they are used in immunolabelling experiments, fluo- tionally cause the tail-to-tail joining of hexameric assem- rescence microscopy and diagnostics. The major organisms blies of these biliproteins to form larger aggregates such as exploited for production are the cyanobacterium Spirulina peripheral rods and core cylinders. Allophycocyanin as- for phycocyanin and the red alga Phorphyridium for semble into phycobilisome core with the assistance of three phycoerythrin (Roman et al. 2002). types of linker polypeptides: the large core-membrane The purpose of the review is to assess the wealth of linker polypeptide (LCM) involved in the interaction of knowledge on the applications of phycobiliproteins and the PBS core with the thylakoids, rod-core linker polypeptides technological backup available for commercial venturing. (LRC) that mediate the attachment of the peripheral rods to This can be envisaged by analyzing application oriented the PBS core and the small core-linker polypeptides (LC) research, patents and commercial activities. A compilation which participate in the assembly of core substructure. The of this knowledge and its analysis will be of immense use peripheral rods of the phycobilisomes are composed of for attaining further improvements. phycoerythrin or phycoerythrocyanin and phycocyanin in association with the appropriate rod-linker polypeptides (LR). Phycoerythrin hexamers of some marine cyanobac- Applied research teria and red algae contain a third type of subunit γPE in the central cavity of the hexamer. These subunits are bifunc- Utility of phycobiliproteins tional phycobiliproteins that act as light harvesting phyco- biliproteins and linker polypeptides (Sidler 1994). The As colorant morphology of phycobilisomes varies with the organisms. These particles may be ellipsoidal, hemidiscoidal, or There is an increasing demand for natural colors which are bundles of rod shaped elements. The differences in gross of use in food, pharmaceuticals, cosmetics, textiles and as morphology do not reflect fundamental differences in the printing dyes. However, their utility is limited to few of placement of the major phycobiliproteins or in the these since the natural dyes have low tinctorial values and fundamental properties of the particle (Glazer 1989). persistence. Due to the toxic effect of several synthetic In contrast to the proteins of the cyanobacteria and of the dyes, there is an increasing preference to use natural colors red algae, the cryptomonad phycobiliproteins are unusual in for various end uses. Phycobiliproteins are used as a natural several ways such as (1) phycobilisomes are lacking due to protein dye in the food industry (C-phycocyanin) and in the the formation of tetrameric complexes and therefore not cosmetic industry (C-phycocyanin and R-phycoerythrin). possible to form phycobilisomes, (2) each species of Phycocyanin derived from Spirulina platensis is used as a cryptomonad contains only one type of phycobiliproteins natural pigment in food such as chewing gum, dairy either phycoerythrin or phycocyanin, (3) the proteins are products and jellies (Santos et al. 2004). Despite its lower found on the lumenal rather than the stromal side of the stability to heat and light, phycocyanin is considered more thylakoid membrane, (4) the proteins form dimers, rather versatile than gardenia and indigo, showing a bright blue J Appl Phycol (2008) 20:113–136 115 color in jelly gum and coated soft candies (Lone et al. accessed as a fluorochrome for flow cytometric immuno- 2005). They are also used in coloring of
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