Research On The Expression Of Phytochrome Protein And The Characterization Analysis Of A-PEC

Phytochrome combined with protein and chromophore was a kind of typicalphoto chromic photoreceptors in the far-infrared light region (R/FR). It waswidespread in the plant, bacteria and cyanobacteria. Cyanobacteria phytochrome wasexisted in the Synechocystis sp.PCC6803. Through the protein structure predictionanalysis finished in the Synechocystis sp.PCC6803gene, we succeed to get slr1212and slr2031gene and their protein. We hoped the protein connected withchromophore and studied the mechanism by spectroscopy analysis.Phycobiliprotein included phycoerythrocyanin(PEC) was a class oflight-harvesting pigment-protein. We studied the reorganized-PEC in thebiosynthesis conditions, factors influencing the stability and stability of pigmentpeptide. The research could be used phycobiliprotein as an important supplement inthe applied research, with economic significance.By molecular biology methods, we transferred-PEC subunit gene into E. colito express the subunit biosynthesis of-PEC. The expression content of reorganized-PEC was up to11.271mg/100mL when it was in the28°C for14h inducedexpression with inducer IPTG for1.0mmol/L condition.We studied the temperature, pH, light, ionic strength, metal ions and smallmolecules and other factors effected on the stability of reorganized-PEC. Resultsshowed that the protein maintained well in the blow37℃, pH4~9, low concentrationof neutral salt and carbohydrates. However the protein was broken by the UVirradiation and most metal ions.We researched the stability factors effected the pigment peptide. Experimentproved that PBS buffer had little effect but multi-alkanols solvent had some influenceon the pigment peptide. Pigment peptide kept for a long time in the methanol.