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Title: Cloning, expression, and characterization of thermotolerant manganese superoxide dismutase from Bacillus sp. MHS47
Authors: Areekit S.
Kanjanavas P.
Khawsak P.
Pakpitchareon A.
Potivejkul K.
Chansiri G.
Chansiri K.
Keywords: 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
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
nucleotide sequence
open reading frame
pH measurement
polyacrylamide gel electrophoresis
polymerase chain reaction
protein expression
sequence alignment
sequence homology
temperature dependence
Bacillus anthracis
Bacillus cereus
Bacillus sp.
Bacillus thuringiensis
Bacterial Proteins
Enzyme Stability
Hydrogen-Ion Concentration
Superoxide Dismutase
Issue Date: 2011
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.
ISSN: 14220067
Appears in Collections:SCOPUS 1983-2021

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