Industrial Production of Superoxide Dismutase (SOD): A Mini Review
Received Date: Aug 01, 2017 / Accepted Date: Aug 08, 2017 / Published Date: Aug 16, 2017
The use of chemical advances to mechanical research, improvement, and assembling has turned into a critical field. Since the creation of rough rennet in 1874, a few catalysts have been marketed, and utilized for restorative, supplementary, and different applications. Late headways in biotechnology now enable organizations to create more secure and more affordable chemicals with upgraded intensity and specificity. Cancer prevention agent catalysts are developing as another expansion to the pool of modern chemicals and are outperforming every single other compound as far as the volume of research and creation. In the 1990s, a cell reinforcement chemical-superoxide dismutase (SOD) was brought into the market. In spite of the fact that the catalyst at first demonstrated extraordinary guarantee in restorative applications, it didn't perform up to desires. Therefore, its utilization was restricted to nontranquilize applications in people and medication applications in creatures. This survey compresses the ascent and fall of SOD at the mechanical level, the purposes behind this, and potential future push territories that should be tended to. The audit likewise concentrates on other modernly significant parts of SOD, for example, mechanical significance, catalyst designing, generation procedures, and process streamlining and scale-up.
Keywords: Antioxidant enzyme, Biotechnology, Superoxide dismutase, Photosynthesis
Oxygen evolving photosynthetic organism especially blue-green algae (Cyanobacteria) has dramatically changed the reducing Earth’s atmosphere  into more oxidant by photolysis of water between 3.2 and 2.4 billion years ago . Which was followed by the build-up and development of aerobic organisms thereby started consuming oxygen (O2) as a strong electron acceptor. As we know that O2 is a strong electron acceptor, it may cause severe damaging effects to the own cells by destabilizing its own metabolism. This happens in live cells due to the generation of reactive oxygen species (ROS) during both the photosynthesis and respiration. The reactive oxygen species are uncontrollably synthesized as an intermediates during O2 reduction (1/2O2) or oxidation (O2-). The most potent and highly ROS are singlet oxygen (1/2O2), superoxide anion (O2-), hydrogen peroxide (H2O2) and the hydroxyl free radical (OH-). The superoxide anion (O2-) and hydroxyl free radical (OH-) are the most reactive ROS with the biomolecules including protein, lipid and nucleic acids due to the occurrence of unpaired electrons.
The hydroxyl free radical is one of the intermediate, generated due to the reaction of O2- with the Fe-S clusters and releases an iron molecule during Fenton reaction . The superoxide anion (O2-) is negatively charged and thus cannot be diffused through membranes and oxidizes [4Fe-4S]2+in to [3Fe-S] 1+ by releasing iron (Fe2+). And thus, Fe2+reacts with H2O2 and resulted in the generation of hydroxyl free radical (OH-).
Fe2++H2O2 → OH-+FeO2+ + H+ → Fe3++OH-+OH
The hydroxyl free radical (OH-) can cause highly damaging effects on DNA neither superoxide anion (O2-) nor hydrogen peroxide (H2O2) but they are the precursors for the proliferative generation of hydroxyl free radicals through Fenton reaction .
To overcome this problem, the living organisms had developed various defence mechanisms to shield themselves against the causing damages by ROS . The Prokaryotic and Eukaryotic organisms have developed various defence mechanisms throughout the course of evolution and are enzymatic and non-enzymatic. Catalases, Superoxide dismutase (SOD) and Peroxidases are enzymatic whether glutathione, carotenoids, vitamins A, C and E etc. are non-enzymatic. The enzymatic mechanism is the primary antioxidant defence evolved within the organism but the non-enzymatic are secondary antioxidant defence consumed as intake from food.
Superoxide Dismutase (SOD)
As the name revels that the enzyme SOD (EC 22.214.171.124) performs the dismutation reaction on the superoxide anions (O2-) generated during the metabolic activities of cells . Generally, the SOD enzyme converts two molecules of superoxide anions (O2-) into hydrogen peroxide (H2O2) and one molecule of oxygen (O2). Followed by the conversion of H2O2 into water molecule by other enzymes like catalase and peroxidases.
2O2-+2H+ → H2O2 + O2
Superoxide dismutase is a primary antioxidant enzyme and ubiquitous in nature present in all kinds of living organisms from Prokaryote to Eukaryote. Different forms of SODs are found and are distinguished based on the metal cofactors present at the active site of the enzyme. Copper and Zinc SOD (Cu/Zn-SOD), Nickel SOD (Ni- SOD), Manganese SOD (Mn-SOD) and Iron SOD (Fe-SOD). The Cu/Zn-SOD reported to occur in the bacterial periplasm, cytoplasm and chloroplast of photosynthetic plants. Superoxide anions (O2-) are impermeable through membrane and thus the Cu/Zn (sod1) SOD is dispersed in diverse locations including nucleus, lysosome, peroxisome and cytosol to detoxify O2-. Extracellular form of Cu/Zn SOD (sod3) is also reported in animals. The SOD3 is different from SOD1 whereas the latter is a homodimer and the former is a homotetramer. The Fe SOD and Mn SOD are found in the Prokaryotes, but the former found in the chloroplast and the latter found in the mitochondria of higher organisms. For the last forty years, approximately 30,000 research articles have been published on the SOD and about 180 patents have been applied on the applications of SOD.
Pharmaceutical applications of SOD
The non-enzymatic antioxidants are the secondary and dietary antioxidants but the availability of such antioxidants is being reduced based on their properties like stability, solubility, isomers, processing with food, biotransformation in the gastrointestinal tract . The induction of oxidative stress due to the generation of ROS leads to the cause of various diseases including cancer, asthma, diabetes, arthritis, atherosclerosis, aging, infertility, neurological disorders, ischemiareperfusion injury, transplant rejection, autoimmune diseases, rheumatoid arthritis, septic shock-induced tissue injury . Various clinical trials have been carried out in humans to hamper and control the ROS by supplementation of SOD and thereby to overcome such diseases. The proliferation of amyotrophic lateral sclerosis (ALS) have been reported due to the mutation in sod gene or its deficiency in human . The expression fold of SOD can be optimized epigenetically in diet, which suppressed the CpG methylation in promoter and thus induced the expression fold of Mn SOD in the vegetarian group when compared with the omnivorous group. Minimal rates of chronic cardiovascular diseases and different types of cancer were reported in vegetarians than the omnivores . Relatively, elevated levels of oxidative stress and suppressed levels of SOD were recorded in people smokes cigarette and drink alcohol . The supplementation of SOD lowering the lactic acid content and hampering fatigue of diaphragm, protection against UV rays, prevent graying of hair, proliferates the growth of hair, heals wounds, reduce wrinkles on face, depigmentation in athletes .
Industrial applications of SOD
SOD formulation is also used along with the production of tobacco based products to minimize the free radical damage occurs in respiratory tract  and which can be reduce the hangover after consumption of alcohol . In former days the SOD was a product from liver and serum of animals (pig, horse, bull and dog etc.) for biochemical purpose. Nowadays, it was also derived from plant sources (seeds, vegetables, cereals and fruits) but due to the minimal amount and high cost extraction methods it was not feasible for commercialization. Thus, the microbial sources were chosen which could be feasible for induction of SOD subjected to ROS stress and the large scale production of SOD. The proliferation of SOD was induced by increase in the air pressure from 1 to 6 bar in a batch cultivation of Yarrowia lipolytica .
Hence, the SOD plays an important role in pathogens to scavenge the extracellular ROS derived from the host defence mechanism. And due to this activity, many research works have been carried out as a target for drugs to protect the host against the pathogens like Plasmodium falciparum , Brucella abortus, Schistosoma mansoni  and antigenic agent in serodiagnosis . It has shown to increase the efficiency of penetration through skin from topical creams, when fused with HIV-1 tat protein transduction domain or lysine-rich peptide . The SOD in combination with chaperone proteins safe guards the proteins from its inhibition by H2O2 and withstand up to 45°C of temperature .
The applications of SOD extended to cosmetic and manufacturing of other supplementary products to protect from free radical damages. Nelson  investigated and reported that SOD can also prolong the survival period of organs for transplantation, sperms  food stuffs  laundry ingredients to remove Amadori and Maillard products  and as biosensors to detect superoxide anions (O2-) . In higher green photosynthetic plants, the SOD used as a shield against physio-chemical stresses including chilling, drought, salinity and high light exposure, O3, metal ions, herbicides respectively thus enhances high yield biomass and its proliferation [24-26]. The food preservatives are subjected to generate ROS to avoid microbial contamination  and the high oxidative stress occurs during fermentation resulted in cell damage and poor productivity of fermented bioproducts. Several microbial sources of SOD have been optimized and characterized from Caulobacter, Brucella, Haemophilus, Pseudomonas and Escherichia coli . The bacterium Lactobacillus fermentum ME-3 strain has been patented for the high SOD activity and also helps in the gastrointestinal and urogenital infections treatment . Several animal and plant derived SODs were expressed using pET30a+vector in E. coli Rosetta DE3 pLysS with tRNAs for certain rare amino acids found in plant and animal SODs.
The famous PPL therapeutics (Netherland) who cloned the sheep Dolly has developed transgenic lambs for SOD production. The purified recombinant human Cu/Zn SOD expressed in E. coli yield up to 5% of Cu/Zn SOD . The SOD3 expressed in pET-28a in E. coli yielded up to 26% of SOD of total cellular protein . The overexpressing of SOD was successfully obtained by multicopy plasmid YG131 in Kluyveromyces marxianus L3 strain . Supplemented with Cu2+ and Zn2+ yielded Cu/Zn SOD with the use of yeast chaperone  and the yield was 30-50% of total bacterial protein with 87-98% Cu saturation. The SOD can be overexpressed in milk through acidic protein (wap) promoter resulting in 0.7 mg/ml and 3 mg/ml in transgenic mice and rabbits respectively [34,35]. The yeast glyceraldehyde phosphate dehydrogenase promoter was used in the high level expression of human SOD in yeast . The bacmid a baculovirus shuttle vector system used as a vector to overexpress Mn SOD in insects like Bombyx mori as a bioreactor . The human liposarcoma (LSA) cells were used as a host for the synthesis of Mn SOD, but astoundingly it was secreted in the medium than being found in the mitochondria. The Chinese hamster ovary expression system yield very low amount of human SOD3 . Recombinant SOD was attained from 0.5 l fed-batch bioreactor with 1.4 × 106 Units in one liter of the medium .
The SOD production from brewer’s yeast was also patented by Suntory Ltd. in Japan . The solid state and submerged fermentation methods obtained up to 2600 U/ml of SOD from Bacillus subtilis strain . The SOD extracted from marine microbe Photobacterium sepia and Photobacterium phosphoreum learnt that it was auspicious to reduce UV-inducced erythema in sportsmen. The final concentration of the enzyme was 10 times high when compared with the yield from baker’s yeast and stable for 2 years under 8°C without retarding its activity. The same drug have shown many pharmaceutical applications in human clinical trials .
Commercially available SOD as drug
Even though there are various sources and forms SOD, bovinederived SOD commonly called as Orgotein available commercially to treat inflammation and radiation induced side-effects. It has been also approved by US-FDA to treat inflammation in cattle and pets and used in the treatment of familial amyotrophic lateral sclerosis (ALS) in 1995. Various patents were owned by Oxis International Inc. for the extraction of orgotein from animals and its therapeutic applications . Superoxide dismutase from marine source is being used in cosmetics by L’oreal and different formulations and manufacturing processes were patented by the same company . The recombinant SOD from yeast have enormous temperature stability up to 45°C and named as Biocell SOD developed by Brooks Industries (USA) in 1987 . The Biocell SOD (0.1-0.5%) is being used in skin care formulations due to its temperature stability when heating and which are available in Arch (NJ, USA) a personal care product.
Nowadays the formulations of SOD are widely used commercially as moisturizes, sunscreens, skin-lightening creams, eye creams, nail polish and anti-hair fall sprays and available in prestigious brands such as Paula’s Choice, Bioelements, Rachel Perry, The Herbarie, Dabao Cosmetics Co. Ltd., Supplement Spot LLC, Nature’s Drugstore, Revitol Corporation, Avenue, Phytomer, Pevonia Botanica Skin Care and Estee Lauder . SOD extract (extramel) from cantaloupe melon have been developed and marketed first by Bionov (France) and which awarded European anti-stress promising ingredient of the year in 2008. The encapsulated formulation of extramel is used as a cosmetic applications by Seppic (France) . Isocell Pharma has developed an oral supplement SOD product Glisodin in combination with wheat Gliadin which not only prevent degradation of SOD in the gastrointestinal tract and also improved its uptake in intestine . The same available as spray-dried powder with 1 U/mg of activity stable for 2 years at below 20°C and the same company has many patents on glisodin applications . The glisodin is also marketed and manufactured by other companies also, the are PL Thomas Inc. (USA), Cell Logic Nutraceutical Solutions (Australia), PT Kalbe Farma Tbk (Indonesia), Syspharma Co. Ltd. (Korea), Millenium Biotechnologies Inc. (NH, USA), Nutrition Act Co. Ltd. (Japan), PURE-XP Ltd. (UK), and Novus Research Inc. (AZ, USA). It is also used in a pet healthpromoting formulation by Nutramax Laboratories Inc. (MD, USA). In human the glisodin is effective in elevating antioxidant levels in serum and minimizes reducing pain in inflammatory conditions like arthritis. The glisodin formulations resurgex and resurgex plus from Millenium Biotechnologies (NH, USA) supplemented to people who are struggling with immunocompromised conditions such as AIDS or cancer  which was confirmed in 6 month clinical study on 25 HIV-1 patients .
Various sources of SOD from both native and recombinant are now commercially available in the form of biochemical reagents from different companies such as Roche, Sigma, Wako, Jena Bioscience, AMS Biotechnology Ltd, Worthington and Calzyme . BTG and Chiron Corporation (CA, USA) received orphan drug designation using Cu/Zn SOD to hamper reperfusion injury in donor organs. Recombinant human SOD yielded more patents to Chiron Corporation (a part of Novartis). And they have performed various methods to improve thermostability, pharmacokinetics and catalytic efficiency of the enzyme .
SOD from blue-green algae
Algae are the large and diverse group of aquatic photosynthetic organisms exists in both the marine and freshwater forms which are ubiquitous in nature. Both microscopic and macroscopic forms of algae are found which are classified as Bacilloriophyceae (Diatoms), Chlorophyta, Euglenophyta, Dinoflagellates, Chrysophyta, Phaeophyta, Rhodophyta and Cyanobacteria. The cyanobacteria are the prokaryotic, photosynthetic microorganisms named due to the production of special blue-green pigment phycocyanin and reddish brown pigment phycoerythrin. The blue-green algae are one among the oxygen evolving microorganisms evolved approximately 3.5 billion years ago as a result of oxygenic photosynthesis. The cyanobacteria are placed in between the prokaryote (anaerobic bacteria) and the eukaryote (green algae) because, they do not have a well-defined nucleus and cell organelles at the same time they are photoautotrophic. The cyanobacteria are the well-known sources of neutraceutical compounds, for example; Spirulina sp. which has easily digestible protein and phycobiliproteins are the products from Synechococcus sp. have high commercial value. The sulfated polysaccharides are recently reported as anti-viral agents extracted from some of the filamentous cyanobacteria e.g., Nostoc sp.
Generally, the cultivation of cyanobacteria is not much more difficult due to fast growth, high photosynthetic efficiency and cheap labor as in Spirulina cultivation. Anabaena and Spirulina are the sources of commercial proteins and vitamins. Especially, the cyanobacteria have the ability of undergoing high degree of O2 reduction by utilizing 50% of photosynthetic electrons, but only 15% is utilized by plants . Some of the previous reports of superoxide dismutase enzymes from cyanobacteria are given in table.
However, SODs from several alternative sources rather than Bovine and recombinant may be effective drug in the near future (Table 1). For example, SODs from Humicola lutea , yeast and Debaryomyces hansenii shown to have protective activity over myeloid Graffi tumor, infection of influenza virus, adjuvant arthritis and carrageenan induced edema in mice [55-57]. The SOD formulations from various sources is the need of the hour research in the pharmaceutical applications due to different properties of different forms of the enzyme.
|2.||Plectonema boryanum UTEX 485|||
|6.||Nostoc PCC 7120|||
|7.||Anabaena variabilis Kutz|||
Table 1: The Superoxide dismutase enzyme (SOD) reported from cyanobacteria.
- Dietrich LE, Tice MM, Newman DK (2006) The co-evolution of life and earth. Curr Biol 16: 395-400.
- Brocks JJ, Logan GA, Buick R, Summons RE (1999) Archean molecular fossils and the early rise of eukaryotes. Science 285: 1033-1036.
- Imlay JA (2003) Pathways of oxidative damage. Annu Rev Microbiol 57: 395-418.
- McCord JM, Fridovich I (1969) Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem 244: 6049-6052.
- Ratnam DV, Ankola DD, Bhardwaj V, Sahana DK, Ravi Kumar MNV (2006) Role of antioxidants in prophylaxis and therapy: a pharmaceutical perspective. J Control Release 113: 189-207.
- McCord JM (1993) Human disease, free radicals, and the oxidant/antioxidant balance. Clin. Biochem 26: 351-357.
- Rabe M, Felbecker A, Waibel S, Steinbach P, Winter P, et al. (2010) The epidemiology of CuZn-SOD mutations in Germany: a study of 217 families. J Neurol 257: 1298-1302.
- Thalera R, Karlica H, Rusta P, Haslberger AG (2009) Epigenetic regulation of human buccal mucosa mitochondrial superoxide dismutase gene expression by diet. Br J Nutr 101: 743-749.
- Russo M, Cocco S, Secondo A, Adornetto A, Bassi A, et al. (2009) Cigarette smoke condensate causes a decrease of the gene expression of Cu–Zn superoxide dismutase, Mn superoxide dismutase, glutathione peroxidase, catalase and free radicalinduced cell injury in SH-SY5Y human neuroblastoma cells. Neurotox Res 19: 49-54.
- Life Extension Magazine (2005) Super oxide dismutase (SOD): boosting your body’s store of the enzyme SOD provides powerful protection against oxidative stress.
- Hersh T, Hersh R (2002) Antioxidants to neutralize tobacco free radicals. US Patent 6415798.
- Diaz VH (2008) Composition including superoxide dismutase and prickly-pear cactus for minimizing and preventing hangovers. US Patent 20080020071.
- Lopes M, Gomes N, Mota M, Belo I (2009) Yarrowia lipolytica growth under increased air pressure: influence on enzyme production. Appl Biochem Biotechnol 159: 46-53.
- Soulere L, Delplace P, Davioud-Charvet E, Py S, Sergheraert C, et al. (2003) Screening of Plasmodium falciparum iron superoxide dismutase inhibitors and accuracy of the SOD-assays. Bioorg Med Chem 11: 4941-4944.
- LoVerde PT, Carvalho-Queirozm C, Cook R (2004) Vaccination with antioxidant enzymes confers protective immunity against challenge infection with Schistosoma mansoni. Mem Inst Oswaldo Cruz 99: 37-43.
- Holdom MD, Lechenne B, Hay RJ, Hamilton AJ, Monod M (2000) Production and characterization of recombinant Aspergillus fumigatus Cu, Zn superoxide dismutase and its recognition by immune human sera. J Clin Microbiol 38: 558-562.
- Park J, Ryu J, Jin LH, Bahn JH, Kim JA, et al. (2002) 9-Polylysine protein transduction domain: enhanced penetration efficiency of superoxide dismutase into mammalian cells and skin. Mol Cells 13: 202-208.
- Bresson-Rival D, Boivin P, Linden G, Perrier E, Humbert G (1999) Stabilized compositions of superoxide dismutase obtained from germinated plant seeds. US Patent 5904921.
- Nelson SK, Bose S, Rizeq M, McCord JM (2005) Oxidative stress in organ preservation: a multifaceted approach to cardioplegia. Biomed Pharmacother 59: 149-157.
- Shizuka T, Mikiko S, Nobuhiko Y, Masaya G, Takashi N, et al. (1999) Superoxide dismutase-like activity of boar semen and effect of SOD on the preservation of boar spermatozoa. Jpn J Swine Sci 36: 42-46.
- Prieels JP, Maschelein C, Heilporn M (1991) Composition for removing oxygen in foodstuff and drinks. US Patent 5010007.
- Maurer KH, O’Connell T, Hoven N, Pruser I, Huchel U, et al. (2008) Use of superoxide dismutases in laundry and cleaning agents. PCT application WO/2008/107346.
- Tian Y, Mao L, Okajima T, Ohsaka T (2002) Superoxide dismutase based third-generation biosensor for superoxide anion. Anal Chem 74: 2428-2434.
- Ahmad R, Kim YH, Kim MD, Kwon SY, Cho K, et al. (2010) Simultaneous expression of choline oxidase, superoxide dismutase and ascorbate peroxidase in potato plant chloroplasts provides synergistically enhanced protection against various abiotic stresses. Physiol Plant 138: 520-533.
- Vyas D, Kumar S (2005) Purification and partial characterization of a low temperature responsive Mn-SOD from tea (Camellia sinensis (L.) O. Kuntze). Biochem Biophys Res Commun 329: 831-838.
- Sahoo R, Kumar S, Ahuja PS (2001) Induction of a new isozyme of superoxide dismutase at low temperature in Potentilla astrisanguinea lodd. variety argyrophylla (Wall, ex. Lehm) Griers. J Plant Physiol 158: 1093-1097.
- Aoyagi H, Ishii H, Ugwu CU, Tanaka H (2008) Effect of heat-generated product from uronic acids on the physiological activities of microbial cells and its application. Bioresour Technol 99: 4534-4538.
- Benov LT, Beyer WF, Jr Stevens RD, Fridovich I (1996) Purification and characterization of the Cu, Zn SOD from Escherichia coli. Free Radic Biol Med 21: 117-121.
- Mikelsaar M, Zilmer M, Kullisaaar T, Annuk H, Songisepp E (2007) Strain of micro-organism Lactobacillus fermentum ME-3 as novel anti-microbiol and anti-oxidative probiotic. US Patent 7244424.
- Hartman JR, Geller T, Yavin Z, Bartfeld D, Kanner D, et al. (1986) High-level expression of enzymatically active human Cu/Zn superoxide dismutase in Escherichia coli. Proc Natl Acad Sci 83: 7142-7146.
- He HJ, Yuan QS, Yang GZ, Wu XF (2002) High-level expression of human extracellular superoxide dismutase in Escherichia coli and insect cells. Protein Expr Purif 24: 13-17.
- Dellomonaco C, Amaretti A, Zanoni S, Pompei A, Matteuzzi D, et al (2007) Fermentative production of superoxide dismutase with Kluyveromyces marxianus. J Ind Microbiol Biotechnol 34: 27-34.
- Ahl IM, Lindberg MJ, Tibell LAE (2004) Coexpression of yeast copper chaperone (yCCS) and CuZn-superoxide dismutases in Escherichia coli yields protein with high copper contents. Protein Expr Purif 37: 311-319.
- Hansson L, Edlund M, Edlund A, Johansson T, Marklund SL (1994) Expression and characterization of biologically active human extracellular superoxide dismutase in milk of transgenic mice. J Biol Chem 269: 5358-5363.
- Stromqvist M, Houdebine M, Andersson JO, Edlund A, Johansson T, et al. (1997) Recombinant human extracellular superoxide dismutase produced in milk of transgenic rabbits. Transgenic Res 6: 271-278.
- Hallewell RA, Mills R, Tekamp-Olson P, Blacher R, Rosenberg S, et al. (1987) Amino terminal acetylation of authentic human Cu, Zn superoxide dismutase produced in yeast. Nature Biotechnology 5: 363-366.
- Yue WF, Li XH, Wu WC, Roy B, Li GL, et al. (2008) Improvement of recombinant baculovirus infection efficiency to express manganese superoxide dismutase in silkworm larvae through dual promoters of Pph and Pp10. Appl Microbiol Biotechnol 78: 651-657.
- Tibell L, Hjalmarsson K, Edlund T, Skogman G, Engstrom A, et al. (1987) Expression of human extracellular superoxide dismutase in Chinese hamster ovary cells and characterization of the product. Proc Natl Acad Sci 84: 6634-6638.
- Raimondi S, Uccelletti D, Matteuzzi D, Pagnoni UM, Rossi M, et al. (2008) Characterization of the superoxide dismutase SOD1 gene of Kluyveromyces marxianus L3 and improved production of SOD activity. Appl Microbiol Biotechnol 77: 1269-1277.
- Asami S, Kusumi T, Amachi T, Yoshizumi H (1987) Process for production of superoxide dismutase. European Patent Application EP 19870218472.
- Hsieh PC, Chuang CY (2008) The production of high-activity superoxide dismutase (SOD) and application in methods of both the solid state and liquid-state fermentation. US Patent Application 20080003641.
- Esco R, Valencia J, Coronel P, Carceller JA, Gimeno M, et al. (2004) Efficacy of orgotein in prevention of late side effects of pelvic irradiation: a randomized study. Int J Radiat Oncol Biol Phys 60: 1211-1219.
- Schulte T, Huber W (1973) Pharmaceutical compositions comprising orgotein and their use. US Patent 3773929.
- Colin C, N’Guyen QL (1999) Cosmetic composition containing, in combination, a superoxide-dismutase and a melanin pigment. US Patent 5925363.
- Lods LM, Dres C, Johnson C, Scholz DB, Brooks GJ (2000) The future of enzymes in cosmetics. Int J Cosmet Sci 22: 85-94.
- Smith WP (1989) Trehalose containing cosmetic composition and method of using it. US Patent 4839164.
- Dreyer A, Ginoux JP, Roch P, Lacan D, Yard C (2006) Cucumis melo extract coated and/or microencapsulated in a fat-soluble agent based on a fatty substance. US Patent 7132118.
- Chenal H, Davit-Spraul A, Brevet J, Legr A, Demouzon J, et al (2006) Restored antioxidant circulating capacities in West African AIDS patients receiving an antioxidant nutraceutical Cucumis melo extract rich in superoxide dismutase activity. XVI International AIDS Conference.
- Dugas B, Calenda A, Sauzieres J, Postaire E (2002) Therapeutic uses of heterologous superoxide dismutase (HSD) and method for selecting said HSD. US Patent 6426068.
- Germano C (2003) Nutrient therapy for immunocompromised patients. US Patent 6503506.
- Business Wire (2004) Advanced medical nutritional supplement shown to improve overall health and wellbeing for HIV/AIDS in clinical trial: resurgex nutritional formula beneficial for HIV patients on HAART therapy.
- Hallewell RA, Bell GI, Mullenbach GT (2001) Manganese superoxide dismutase cloning and expression in microorganisms. US Patent 6326003.
- Getzoff ED, Cabelli DE, Fisher CL, Parge HE, Viezzoli MS, et al. (1992) Faster superoxide dismutase mutants designed by enhancing electrostatic guidance. Nature 358: 347-351.
- Badger MR, Von CS, Ruuska S, Nakano H (2000) Electron flow to oxygen in higher Plants and Algae: rates and control of direct Photoreduction (Mehler reaction) and Rubsico Oxygenase. Philos Trans R Soc Lond B Biol Sci 355: 1433-1446.
- Angelova M, Dolashka-Angelova P, Ivanova E, Serkedjieva J, Slokoska L, et al. (2001) A novel glycosylated Cu/ Zn-containing superoxide dismutase: production and potential therapeutic effect. Microbiology 147: 1641-1650.
- Garcia-Gonzalez A, Ochoa JL (1999) Anti-inflammatory activity of Debaryomyces hansenii Cu, Zn-SOD. Arch Med Res 30: 69-73.
- Ratcheva I, Stefanova Z, Vesselinova A, Nikolova S, Kujumdjieva A, et al. (2000) Treatment of adjuvant arthritis in mice with yeast superoxide dismutase. Pharmazie 55: 533-537.
- Asada K, Yoshikawa K, Takahashi M, Maeda Y, Enmanji K (1975) Superoxide dismutases from a blue-green alga, Plectonema boryanum. J Biol Chem 250: 2801-2807.
- Campbell WS, Laudenbach DE (1995) Characterization of four Superoxide dismutase genes from a filamentous Cyanobacterium. Journal of Bacteriology 177: 964-972.
- Landis E, Henry A, Gogotov IN, Hall DO (1978) Superoxide dismutase and Catalase in the protection of the Proton-donating systems of nitrogen fixation in the Blue-green alga Anabaena Cylindrica. Biochem J 174: 373-377.
- Shirkey B, Kovarcik DP, Wright DJ, Wilmoth G, Prickett TF, et al (2000) Active Fe-Containing Superoxide Dismutase and Abundant sodF mRNA in Nostoc commune(Cyanobacteria) after Years of Desiccation. J Bacteriol 182: 189-197.
- Canini A, Leonardi D, Caiola MG (2001) Superoxide dismutase activity in the Cyanobacterium Microcystis aeruginosa after surface bloom formation. New Phytologist 152: 107-116.
- Regelsberger G, Laaha U, Dietmann D, Ruker F, Canini A, et al. (2004) The Iron Superoxide dismutase from the filamentous Cyanobacterium Nostoc PCC 7120: localization, overexpression and biochemical characterization. J Biol Chem 279: 44384-44393.
- Padmapriya V, Anand N (2010) The influence of metals on the Antioxidant Enzyme, Superoxide Dismutase, present in the Cyanobacterium, Anabaena variabilis Kütz. Journal of Agricultural and Biological Science 5: 4-9.
Citation: Gopal RK, Elumalai S (2017) Industrial Production of Superoxide Dismutase (SOD): A Mini Review. J Prob Health 5:179. Doi: 10.4172/2329-8901.1000179
Copyright: © 2017 Gopal RK, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Select your language of interest to view the total content in your interested language
Share This Article
7th International Conference and Exhibition on Probiotics, Functional and Baby Foods
July 18-19, 2018 Prague, Czech Republic
28th World Nutrition Congress
August 9- 10 2018 Manila, Philippines
8th Annual Congress on Probiotics & Functional Foods
September 24-25, 2018 Tokyo, Japan
- Total views: 1272
- [From(publication date): 0-2017 - Jun 19, 2018]
- Breakdown by view type
- HTML page views: 1148
- PDF downloads: 124