title: Single step aqueous two-phase extraction for downstream processing of C-phycocyanin from Spirulina platensis.
abstract: C-phycocyanin, a natural food colorant, is gaining importance worldwide due to its several medical and pharmaceutical applications. In the present study, aqueous two-phase extraction was shown to be an attractive alternative for the downstream processing of C-phycocyanin from Spirulina platensis. By employing differential partitioning, C-phycocyanin selectively partitioned to the polymer rich (top) phase in concentrated form and contaminant proteins to the salt rich (bottom) phase. This resulted in an increase in the product purity (without losing much of the yield) in a single step without the need of multiple processing steps. Effect of process parameters such as molecular weight, tie line length, phase volume ratio, concentration of phase components on the partitioning behavior of C-phycocyanin was studied. The results were explained based on relative free volume of the phase systems. C-phycocyanin with a purity of 4.32 and yield of about 79 % was obtained at the standardized conditions.
authors.affiliation: Molecular Biology and Genetics Unit, Jawaharlal Nehru centre for Advanced Scientific Research, IISc Campus, Jakkur, Bangalore, 560 064 India.
authors.forename: S
authors.initials: S
authors.lastname: Chethana
authors.affiliation: Dayanada Sagar College of Engineering, Bangalore, India.
authors.forename: Chetan A
authors.initials: CA
authors.lastname: Nayak
authors.affiliation: Department of Food Engineering, CSIR-Central Food Technological Research Institute (CFTRI), Mysore, 570 020 India.
authors.forename: M C
authors.initials: MC
authors.lastname: Madhusudhan
authors.affiliation: Department of Food Engineering, CSIR-Central Food Technological Research Institute (CFTRI), Mysore, 570 020 India.
authors.forename: K S M S
authors.initials: KS
authors.lastname: Raghavarao
keywords: Aqueous two-phase systems; C-phycocyanin; Partition coefficient; Purification; Relative free volume
references.citation: Biochem Biophys Res Commun. 2000 Nov 2;277(3):599-603
references.pmid: 11062000
references.citation: Curr Protein Pept Sci. 2003 Jun;4(3):207-16
references.pmid: 12769719
references.citation: Bioprocess Biosyst Eng. 2008 Aug;31(5):477-82
references.pmid: 18219495
references.citation: Methods Enzymol. 1990;182:19-23
references.pmid: 2314236
references.citation: Biochemistry. 1963 Mar-Apr;2:375-82
references.pmid: 13939643
references.citation: J Biotechnol. 2003 Apr 10;102(1):55-9
references.pmid: 12668314
references.citation: J Pharm Pharmacol. 2000 Apr;52(4):367-8
references.pmid: 10813544
references.citation: J Chromatogr A. 2006 Sep 15;1127(1-2):76-81
references.pmid: 16782107
references.citation: Bioresour Technol. 2007 May;98(8):1629-34
references.pmid: 16962771
references.citation: Adv Biochem Eng Biotechnol. 1992;47:89-135
references.pmid: 1456110
references.citation: Bioresour Technol. 2009 Feb;100(4):1663-9
references.pmid: 18954974
references.citation: Protein Expr Purif. 2005 Apr;40(2):248-55
references.pmid: 15766866
references.citation: Biochem Biophys Res Commun. 2000 Aug 18;275(1):20-5
references.pmid: 10944434
references.citation: Phytochemistry. 2006 Nov;67(22):2424-30
references.pmid: 16973186