Publication:
Cloning, expression, and characterization of thermotolerant manganese superoxide dismutase from Bacillus sp. MHS47

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Issued Date

2011

Resource Type

Article

File Type

application/pdf

ISSN

14220067

DOI

10.3390/ijms12010844

Other identifier(s)

2-s2.0-79251636317

Rights Holder(s)

Scopus

Bibliographic Citation

International Journal of Molecular Sciences. Vol 12, No.1 (2011), p.844-856

Suggested Citation

Areekit S., Kanjanavas P., Khawsak P., Pakpitchareon A., Potivejkul K., Chansiri G., Chansiri K. Cloning, expression, and characterization of thermotolerant manganese superoxide dismutase from Bacillus sp. MHS47. International Journal of Molecular Sciences. Vol 12, No.1 (2011), p.844-856. doi:10.3390/ijms12010844 Retrieved from: https://hdl.handle.net/20.500.14740/7416

Title

Cloning, expression, and characterization of thermotolerant manganese superoxide dismutase from Bacillus sp. MHS47

Author(s)

Areekit S.
 Kanjanavas P.
 Khawsak P.
 Pakpitchareon A.
 Potivejkul K.
 Chansiri G.
 Chansiri K.

Abstract

A superoxide dismutase gene from thermotolerant Bacillus sp. MHS47 (MnSOD47) was cloned, sequenced, and expressed. The gene has an open reading frame of 612 bp, corresponding to 203 deduced amino acids, with high homology to the amino acid sequences of B. thuringiensis (accession no. EEN01322), B. anthracis (accession no. NP_846724), B. cereus (accession no. ZP_04187911), B. weihenstephanensis (accession no. YP_001646918), and B. pseudomycoides. The conserved manganese-binding sites (H28, H83, D165, and H169) show that MnSOD47 has the specific characteristics of the manganese superoxide dismutase (MnSOD) enzymes. MnSOD47 expressed an enzyme with a molecular weight of approximately 22.65 kDa and a specific activity of 3537.75 U/mg. The enzyme is active in the pH range 7-8.5, with an optimum pH of 7.5, and at temperatures in the range 30-45 °C, with an optimum temperature of 37 °C. Tests of inhibitors and metal ions indicated that the enzyme activity is inhibited by sodium azide, but not by hydrogen peroxide or potassium cyanide. These data should benefit future studies of MnSODs in other microorganisms and the biotechnological production of MnSOD47, and could also be used to develop a biosensor for the detection of antioxidants and free radical activity. In the future, this basic knowledge could be applicable to the detection of cancer risks in humans and therapeutic treatments. © 2010 by the authors; licensee MDPI, Basel, Switzerland.

Subject(s)

Bacterial enzyme
 Genomic DNA
 Hydrogen peroxide
 Manganese superoxide dismutase
 Manganese superoxide dismutase 47
 Potassium cyanide
 Recombinant enzyme
 Sodium azide
 Unclassified drug
 Bacterial protein
 Superoxide dismutase
 Article
 Bacillus
 Bacillus anthracis
 Bacillus cereus
 Bacillus pseudomycoides
 Bacillus thuringiensis
 Bacillus weihenstephanensis
 Bacterial gene
 Bacterial strain
 Binding site
 Controlled study
 DNA sequence
 Enzyme activation
 Enzyme activity
 Enzyme analysis
 Enzyme inhibition
 Enzyme purification
 Enzyme stability
 Escherichia coli
 Gene expression
 Gene identification
 Gene isolation
 Genetic analysis
 Genetic code
 Heat tolerance
 Molecular cloning
 Molecular weight
 Nonhuman
 Nucleotide sequence
 Open reading frame
 PH measurement
 Polyacrylamide gel electrophoresis
 Polymerase chain reaction
 Protein expression
 Sequence alignment
 Sequence homology
 Temperature dependence
 Chemistry
 Enzymology
 Genetics
 Metabolism
 PH
 Temperature
 Bacillus anthracis
 Bacillus cereus
 Bacillus sp.
 Bacillus thuringiensis
 Bacillus
 Bacterial Proteins
 Enzyme Stability
 Hydrogen-Ion Concentration
 Superoxide Dismutase
 Temperature

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URI

https://hdl.handle.net/20.500.14740/7416

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Scopus: Year 1983-2021

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