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Current Trends in Biotechnology and Pharmacy Vol. 6 (2) 229-240 April 2012, ISSN 0973-8916 (Print), 2230-7303 (Online) 26. Miranda, M.C., Van Beers, M.M.C., Sauerborn, M., Gilli, F., Hermeling, S., Brinks, V., Schellekens, H. and Jiskoot, W. (2010). Hybrid transgenic immune tolerant mouse model for assessing the breaking of B cell tolerance by human interferon beta. J Immunol Methods, 352:32-37. 27. Perry, R. and Kwang, N. (2006). Monofunctional polyethylene glycol aldehydes. USA patent 7041855. 28. Aghajani-Lazarjani, H., Vasheghani- Farahani, E., Shojaosadati, S.A., Hashemi- Najafabadi, S., Zahediasl, S., Tairahi, T. and Atyabi, F. (2010). The effect of two different polyethylene glycol (PEG) derivatives on the immunological response of PEG grafted pancreatic islets. J Artif Organs, 13:218- 224. 29. Barani, L., Vasheghani-Farahani, E., Aghajani-Lazarjani, H., Hashemi- Najafabadi, S. and Atyabi, F. (2010). Effect of molecular mass of methoxypoly(ethylene glycol) activated with succinimidyl carbonate on camouflaging pancreatic islets. Biotechnol Appl Biochem, 57:25-30. 30. Diwan, M. and Park T.G., (2003). Stabilization of recombinant interferon-by pegylation for encapsulation in PLGA microspheres. Int J Pharm, 252:111-122. Ahmad Abolhasani et al 240 31. Koops, B.C., Verheij, H.M., Slotboom, A.M. and Eegmond, M.R. (1999). Effect of chemical modification on the activity of lipases in organic solvent. Enzyme Microbial Technol, 25:622-631. 32. Davies, L. (1993) Efficiency in Research, Development, and Production: the Statistical Design and Analysis of Chemical Experiments, pp. 1-88. Royal Society of Chemistry, Cambridge 33. Jevsevar, S., Kunstelj, M. and Porekar, V.C. (2010). PEGylation of therapeutic proteins: review. Biotechnol J, 5:113-128. 34 Roy, R.K. (1990) A Prime on the Taguchi Method, Van Nostrand Reinhold, New York, pp. 1-155. 35. Wang, Y.S., Youngster, S., Bausch, J., Zhang, R., McNemar, C. and Wyss, D.F. (2000). Identification of the major positional isomer of pegylated interferon alpha-2b. Biochem, 39:10634–10640. 36. Grace, M., Youngster, S., Gitlin, G., Sydor, W. Xie, L., Westreich, L., Jacobs, S., Brassard, D., Bausch, J. and Bordens, R. (2001). Structural and biological characterization of pegylated recombinant IFN-á-2b. J Interferon Cytokine Res, 21:1103–1115.
Current Trends in Biotechnology and Pharmacy Vol. 6 (2) 241-254 April 2012, ISSN 0973-8916 (Print), 2230-7303 (Online) Enhanced Production of Glutathione from Saccharomyces Cerevisiae using Metabolic Precursor and Purification with New Approach Parbatsingh Rajpurohit, Ashwini Tilay, Shrikant Survase and Uday Annapure* Food Engineering and Technology Department, Institute of Chemical Technology, Matunga, Mumbai 400 019, India *For Correspondence - us.annapure@ictmumbai.edu.in Abstract This paper reports on the enhanced fermentative production of glutathione by Saccharomyces cerevisiae NCIM 3454 using a statistical approach and its successive purification by alternative technique. In the first step, one factor at-a-time method was used to examine the effect of carbon sources, nitrogen sources and pH on glutathione (GSH) production. Subsequently, statistical mathematical model was used to identify the optimum concentrations of the key nutrients for higher GSH production. Glutathione production increased significantly from 55.28 to 148.45 mg/L when Saccharomyces cerevisiae NCIM 3454 was cultivated using optimized medium, as compared to basal medium. Further, glutathione production was considerably increased to 163.12 mg/L by using cysteine amino acid as one of the metabolic precursor. In this study aqueous two phase system (ATPS) was found to be most useful technique to abolish contaminating proteins in glutathione purification. Further enhanced purification was carried out by adsorption chromatography (ion exchange) using a variety of Amberlite resins. Keywords: Glutathione, Saccharomyces cerevisiae, fermentation, precursor, chromatography. Introduction Glutathione (α-glutamyl-L-cysteinylglycine, GSH) is the most abundant water soluble non- Enhanced Production of Glutathione 241 protein consisting of thiol group which is widely distributed in living organisms and predominantly, in eukaryotic ells (1). It functions in many cellular processes including the protection of cells against xenobiotics, carcinogens, radiation and reactive oxygen species (2,3) hence it has medicinally important value in areas like health care, functional foods, cosmetics and its commercial demand is intensifying (4). Other functions of GSH include storage and transport of cysteine, regulation of cell proliferation, synthesis of deoxyribonucleotides, and regulation of leukotriene and prostaglandin metabolism (5). It also works as a neurotransmitter, neuromodulator and regulator in cell proliferation and apoptosis (6). An imbalance of GSH is observed in a wide range of pathologies including, cancer, neurodegenerative disorders, cystic fibrosis, HIV and aging. Normally, most of the glutathione is present in the reduced form GSH while several additional forms of glutathione are present in (microbial) cells, tissues, and plasmas. Oxidized form of glutathione (glutathione disulfide, GSSG) upon oxidation of GSH, can in turn be reduced to GSH by glutathione reductase at the expense of NADPH (7). It is less easily oxidized than its precursors, cysteine and ã-glutamyl cysteine (8). It can be produced by using chemical synthesis (9) enzymatic methods (10) or by direct fermentative methods (11, 12). Although production of GSH by enzymatic method gives maximum concentration (up to 9 g/L) but
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