Cloning of a C-phycocyanin Alpha Subunit from Thermosynechococcus sp. TUBT-T01 and Prediction of Its Properties

C-Phycocyanin, a blue-colored and water soluble protein, is a class of phycobiliproteins that are the major light-harvesting pigments of a photosynthetic system in cyanobacteria. C-phycocyanins are utilized in many industries, including as natural colorants in food and cosmetics and as antioxidant compounds. However, the uses of C-phycocyanins have been limited due to their vulnerability to high temperatures. Therefore, the objective of this study was to identify and analyze the C-phycocyanin gene isolated from Thermosynechococcus sp. TUBT-T01, living in a hot spring in Surat Thani province, in the hope that this C-phycocyanin exhibited thermostable properties and that their applications could be expanded over a wide range of industries. In the present study, the polymerase chain reaction of the gene encoding alpha subunits of C-phycocyanin (cpcA) was performed, using primers designed based upon the sequence alignments of cpcA from Thermosynechococcus sp. available in the GenBank database. The putative cpcA, with an approximate size of 500 base pairs, was detected on an agarose gel. The DNA sequencing analysis indicated that the cpcA was 489 base pairs in length, and its nucleotide sequence was 94 % identical to those of thermophilic Thermosynechococcus sp. NK55, T. elongatus BP-1, and Synechococcus vulcanus. The deduced amino acid sequence was very similar to those of Thermosynechococcus sp. NK55, T. elongatus BP-1, and S. vulcanus. The data derived from the homologous model revealed that the presence of Asp28, Lys32, and Ser72 in the alpha subunit of C-phycocyanin from Thermosynechococcus sp. TUBT-T01 could provide the high thermostability property of this protein.