Abstract:
:A superoxide dismutase (SOD) was purified from Spirulina platensis sonicate. The SOD was purified to homogeneity (48-fold and 0.24% yield) through ammonium sulphate precipitation and DEAE-52 anion exchange chromatography. The SOD from S. platensis appeared to be a homodimer with a molecular weight of 30 kDa and a subunit MW of 15 kDa as determined by both native polyacrylamide gel electrophoresis and mass spectrometry. The enzyme activity was stable at pH 6.5-10.0 and 50 °C. Using group-specific chemical modifying reagents, the amino acids arginine, histidine, tryptophan, tyrosine and aspartic acid were identified to be essential for S. platensis SOD activity. The amino acid composition was found to lack methionine and cysteine. The inhibition of activity by H2O2 suggests that the enzyme may be an iron containing SOD.
journal_name
World J Microbiol Biotechnoljournal_title
World journal of microbiology & biotechnologyauthors
Desai K,Sivakami Sdoi
10.1007/s11274-007-9413-8subject
Has Abstractpub_date
2007-12-01 00:00:00pages
1661-6issue
12eissn
0959-3993issn
1573-0972pii
10.1007/s11274-007-9413-8journal_volume
23pub_type
杂志文章abstract::Psychrophiles are organisms that thrive in cold environments. One of the strategies for their cold adaptation is the ability to synthesize cold-adapted enzymes. These enzymes usually display higher catalytic efficiency and thermolability at lower temperatures compared to their mesophilic and thermophilic counterparts....
journal_title:World journal of microbiology & biotechnology
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journal_title:World journal of microbiology & biotechnology
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journal_title:World journal of microbiology & biotechnology
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