Purification and characterization of superoxide dismutase from Aerobacter aerogenes.

Kim, Si‐Wan; Lee, Sang Ok; Lee, Tae Ho

doi:10.1271/bbb1961.55.101

Cited by 14 publications

(6 citation statements)

References 2 publications

(1 reference statement)

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“…Superoxide Dismutase (SOD) Activity and SOD Induction. SOD determination was performed by the method of Kim et al (1991). Three-tenths of a milliliter of intracellular cell-free extract, 1 mL of EDTA (1 mM), 0.3 mL of epinephrine (0.3 mM, pH 2), and 2 mL of sodium carbonate (0.05 M) were mixed together.…”

Section: Bacterial Strainsmentioning

confidence: 99%

Antioxidative Ability of Lactic Acid Bacteria

Lin

Yen

1999

J. Agric. Food Chem.

440

257

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Nineteen strains of lactic acid bacteria were investigated for antioxidative activity. These includedLactobacillus acidophilus B, E, N1, 4356, LA-1, and Farr; Lactobacillus bulgaricus 12 278, 448, 449, Lb, 1006, and 11 842; Streptococcus thermophilus 821, MC, 573, 3641, and 19 987; and Bifidobacterium longum B6 and 15 708. Intracellular cell-free extract of all strains demonstrated antioxidative activity with inhibition rates of ascorbate autoxidation in the range of 7-12%. Antioxidative mechanisms including metal ion chelating ability, scavenge of reactive oxygen species, enzyme inhibition, and reducing activity of intracellular cell-free extract of lactic acid bacteria were studied. S. thermophilus 821 had the highest metal ion chelating ability for Fe(2+), and B. longum 15 708 showed the highest Cu(2+) chelating ability among the 19 strains tested. All strains demonstrated reactive oxygen species scavenging ability. L. acidophilus E showed the highest hydroxyl radical scavenging ability, and B. longum B6 had the best hydrogen peroxide scavenging ability. Reducing activity was also found in all strains. Most of the strains tested demonstrated excellent reducing activity. B. longum B6 showed the highest reducing activity among the 19 strains tested. In enzyme inhibition, superoxide dismutase activity was not found in these 19 strains, and the activity of superoxide dismutase was not induced when metal ion Mn(2+), Fe(2+), or Cu(2+)Zn(2+) was present.

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Section: Bacterial Strainsmentioning

confidence: 99%

Antioxidative Ability of Lactic Acid Bacteria

Lin

Yen

1999

J. Agric. Food Chem.

440

257

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“…Modifications of purified chicken heart SOD by covalent attachment of GDA chains produce a complex product which displays heterogeneity in both the size and charge of the resulting species. However, the pH dependence of the FeSOD stability of Aerobacter aerogenes remained comparatively stable at alkaline pH in the range of 7.0-11.0 but was rapidly inactivated below pH 7.0 (Kim et al, 1991). The activity variations of purified SOD depend on pH having a maximum in alkaline region at 8.8.…”

Section: Discussionmentioning

confidence: 95%

Dismutation Properties of Purified and GDA Modified CuZnSOD from Chicken Heart

Demirel

Tarhan

2004

Artificial Cells, Blood Substitutes, and Biotechnology

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Superoxide dismutase (SOD, 1.15.1.1) from chicken heart has been purified 139-fold with specific activity of 2130 IU/mg. Purified SOD has a molecular weight 31.0 +/- 1.0 kDa and is composed of two equally sized subunits each having 1.1 +/- 0.03 and 0.97 +/- 0.02 atoms of Cu and Zn elements, respectively. Purified CuZnSOD modified by covalent attachment of the glutaraldehyde (GDA) in presence and absence of bovine serum albumin (BSA). The optimum conditions were obtained with a series of modification reactions as 0.25 mg/mL CuZnSOD in 50 mM phosphate buffer, pH 7.5 containing 3% GDA in presence and absence of 0.25 mg/mL BSA. The highest recovery activity of modified SODs was determined as 23.4 and 18.5% for the designated SOD-I and SOD-II derivatives, respectively. The recovery activity of SOD-I reached 28.6% while SOD-II didn't change significantly and determined as 19% after the reaction with 1% ethylendiamine. The activity variations of native and modified CuZnSODs were investigated depending on the pH and temperature. Optimum pH values for native and modified SOD-I, -II were determined as 8.8, 8.3, and 8.2, respectively. The native and modified SODs have the same optimum temperatures approximately as 35 degrees C. The pH- and thermal-stability properties of modified SODs were found to be better than native SOD, in the pH range of 6.5-8.5 at 25 degrees C after 6 h, and up to 40 degrees C at pH 7.4 after 3 h incubation period. Inhibitory effects of ditiothreitol (DTT), beta-mercaptoethanol, and iodoacetamide were not observed on the native and modified SODs activities after 5 h incubation period. Phenylmethylsulfonylfloride (PMSF), H20O2, and EDTA were caused by slight inhibition on the enzyme activities.

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“…Maximum activity was observed between pH 7.0 to 9.0 at 250ºC [23]. SOD of Neurosporo crassa [24], and yeast [14,25] had a molecular weight of about 32 kDa. Generally, Cu-Zn SODs are stable at neutral pH [11,14] The pH dependence of the Fe-SOD stability of Aerobacter aerogenesis, remained comparatively stable at alkaline pH 7.0-11.0, but was rapidly inactivated below pH 7.0 [26].…”

Section: Discussionmentioning

confidence: 95%

Purification and Characterization of Superoxide Dismutase Isolated From Sewage Isolated E. coli

M¹

2013

Microb Biochem Technol

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Superoxide dismutase (SOD), which plays a very important role in protecting organisms from oxygen toxicity, has therapeutic importance. It was purified from sewage isolated E. coli and characterized. Eukaryotic cells also produce SOD but culturing and maintenance of eukaryotic cells for production of SOD is costly as well as difficult. Using prokaryotic cells i.e. bacteria, production cost can be reduced. A rich bacterial source was identified. Bacterial membrane was ruptured in the presence of lysozyme and glass bead. Following ammonium sulphate precipitation, SOD-containing solution was applied to DEAE-cellulose and then Sephadex G-75 gel columns. SOD was purified 63.91-fold with a specific activity of 3835U/ mg. The molecular weight was estimated to be 35.713 kDa by SDS-PAGE gel. Maximum SOD activity was observed between pH 7.0 to 7.5 at temperature range 37-50ºC. This enzyme has fair thermal stability. The enzyme was found to be stable in presence of 1% salt only. The activity found to be gradually reduced approximately 50% at higher concentrations. It was totally inactivated above 9% salt concentration.

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Purification and characterization of superoxide dismutase from Aerobacter aerogenes.

Cited by 14 publications

References 2 publications

Antioxidative Ability of Lactic Acid Bacteria

Antioxidative Ability of Lactic Acid Bacteria

Dismutation Properties of Purified and GDA Modified CuZnSOD from Chicken Heart

Purification and Characterization of Superoxide Dismutase Isolated From Sewage Isolated E. coli

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