A novel, thermostable manganese-containing superoxide dismutase from Bacillus licheniformis

Boyadzhieva, Ivanka; Atanasova, Miroslava; Эмануилова, Э.

doi:10.1007/s10529-010-0368-8

Cited by 21 publications

(9 citation statements)

References 8 publications

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“…Even at 80°C, SOD NG2215 remained 52% active after 10 min and almost maintained at this level until 60 min. SOD r , the NTD fused SODA BSn5 , also exhibited good thermostability (retained 80% and 61% active at 50°C and 60°C, respectively, after 60 min), indicating that this enzyme acted more like a moderate thermophilic Mn-SOD from B. licheniformis 20 .…”

Section: Resultsmentioning

confidence: 99%

“…Fortunately, the isolation of thermostable SODs from thermotolerant or thermophilic microorganisms offers a rapid and effective means to address this issue. To date, many thermostable SODs have been identified from thermophiles and hyperthermophiles, such as Aquifex pyrophilus 13 , Sulfolobus solfataricus 14 , Aeropyrum pernix 15 , Pyrobaculum aerophilum 16 , Bacillus stearothermophilus 17 , Chloroflexus aurantiacus 18 , Thermomyces lanuginosus 19 , Bacillus licheniformis 20 , Chaetomium thermophilum 21 , and Thermus thermophilus 22 . Recent efforts to improve the thermal resistance of SODs through chemical modification, gene recombination, and simulated SOD compounds have achieved considerable success 23 24 .…”

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confidence: 99%

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A novel mechanism of protein thermostability: a unique N-terminal domain confers heat resistance to Fe/Mn-SODs

Wang

Zhang

et al. 2014

Sci Rep

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Superoxide dismutases (SODs), especially thermostable SODs, are widely applied in medical treatments, cosmetics, food, agriculture, and other industries given their excellent antioxidant properties. A novel thermostable cambialistic SOD from Geobacillus thermodenitrificans NG80-2 exhibits maximum activity at 70°C and high thermostability over a broad range of temperatures (20–80°C). Unlike other reported SODs, this enzyme contains an extra repeat-containing N-terminal domain (NTD) of 244 residues adjacent to the conserved functional SODA domain. Deletion of the NTD dramatically decreased its optimum active temperature (OAT) to 30°C and also impaired its thermostability. Conversely, appending the NTD to a mesophilic counterpart from Bacillus subtilis led to a moderately thermophilic enzyme (OAT changed from 30 to 55°C) with improved heat resistance. Temperature-dependant circular dichroism analysis revealed the enhanced conformational stability of SODs fused with this NTD. Furthermore, the NTD also contributes to the stress resistance of host proteins without altering their metal ion specificity or oligomerisation form except for a slight effect on their pH profile. We therefore demonstrate that the NTD confers outstanding thermostability to the host protein. To our knowledge, this is the first discovery of a peptide capable of remarkably improving protein thermostability and provides a novel strategy for bioengineering thermostable SODs.

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Section: Resultsmentioning

confidence: 99%

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confidence: 99%

A novel mechanism of protein thermostability: a unique N-terminal domain confers heat resistance to Fe/Mn-SODs

Wang

Zhang

et al. 2014

Sci Rep

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“…Among bacterial SODs, the present demand of medical, pharmaceutical and cosmetics industry is thermostable SODs as the production processes involve high temperature and stability is lost. Researchers have tried to explore thermostable SODs and some have achieved success (Boyadzhieva et al, 2010) but no attempt has been made for production process optimization for bulk recovery of enzyme. In the present piece of work, natural thermal habitat, i.e., hot water springs of Himalayan region have been explored for thermostable SOD.…”

Section: Discussionmentioning

confidence: 99%

Statistical augmentation of thermostable Superoxide dismutase (SOD) production from Bacillus licheniformis SPB-13 of Himalayan ranges

Thakur¹,

Pradeep²,

Kumari³

et al. 2020

afjbs

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Background:Aging is a natural phenomenon in all organisms. The pace of aging and related manifestations depends on balance of formation and dismutation of reactive oxygen species (ROS) in the cell. Superoxide dismutase (SOD; EC 1.15.1.1) is an antioxidative enzyme that prevents the aerobic organisms from oxidative damage caused by free radicals that are generated during oxygen metabolism. This enzyme system is the key biomolecule of the cells having antiaging properties and increases the life span of organisms. Objective: The aim of present research was to isolate thermostable SOD producing bacterial strain and to increase its activity by optimizing the production and assay parameters for thermophilic bacterium using response Surface Methodology (RSM) and its identification and phylogenetic analysis using molecular techniques. Materials and Methods: The water and soil samples were collected from thermal springs of different regions of Western Himalayas of India. Out of total 40 isolates, Bacillus sp. SPB-13 was screened for production of SOD on the basis of highest activity and identified using 16s rRNA gene sequencing. One Variable at a Time (OVAT) approach followed by central composite design was employed to analyze the effect of different media and reaction components, i.e., Glucose, casein, yeast extract, NaCl, buffer system, reaction temperature and enzyme concentration on SOD production. Results: One hyperproducer of SOD was isolated and found to be Bacillus licheniformis SPB-13 (NCBI Accn. No. KX185731). Enzyme activity was enhanced from 80 U/mL to 120 U/mL after production and reaction process optimization. A significant increase in SOD activity of 40 U/mL was obtained after classical and statistical optimization. SOD remained fully active at 70°C and after metallotyping, found to be a member of Fe/Mn SOD family. Conclusion: Bacillus licheniformis SPB-13 produces a thermostable SOD with very good antioxidant activity. The production and reaction parameters have been optimized completely using classical and analytical methods to cut the production cost and to increase the yield of SOD. The antiaging potential of this enzyme can be exploited in cosmetics and pharma industry for antioxidative formulations and topical ointments.

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“…40 The thermal stability of enzymes is a desirable feature for industrial applications that require high temperatures to develop products. 41 In species adapted to different thermal regimes, the kinetic properties of enzymes are typically correlated with environmental temperatures, but the correlation between adaptation temperature and enzyme thermal stability is less clear. 42 Studies on coldadapted enzymes revealed higher structural flexibility, which can accommodate the substrate and transport the enzyme into the activated state with minimum loss of energy.…”

Section: Discussionmentioning

confidence: 99%

Copper, zinc superoxide dismutase from Caragana jubata : A thermostable enzyme that functions under a broad pH and temperature window

Kumar

Sharma

Bhardwaj

et al. 2016

Process Biochemistry

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A novel, thermostable manganese-containing superoxide dismutase from Bacillus licheniformis

Cited by 21 publications

References 8 publications

A novel mechanism of protein thermostability: a unique N-terminal domain confers heat resistance to Fe/Mn-SODs

A novel mechanism of protein thermostability: a unique N-terminal domain confers heat resistance to Fe/Mn-SODs

Statistical augmentation of thermostable Superoxide dismutase (SOD) production from Bacillus licheniformis SPB-13 of Himalayan ranges

Copper, zinc superoxide dismutase from Caragana jubata : A thermostable enzyme that functions under a broad pH and temperature window

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