TY - JOUR
T1 - The AlnB protein of the bioemulsan alasan is a peroxiredoxin
AU - Bekerman, R.
AU - Segal, G.
AU - Ron, E. Z.
AU - Rosenberg, E.
N1 - Funding Information:
Acknowledgements This investigation was supported by the Pasha Gol Chair for Applied Microbiology, the Manja and Morris Leigh Chair in Biophysics and Biotechnology, and European Community project COMMODE.
PY - 2005/2
Y1 - 2005/2
N2 - The bioemulsifier of Acinetobacter radioresistens KA53, referred to as alasan, is a high molecular weight complex of a polysaccharide and three proteins (AlnA, AlnB and AlnC). AlnA has previously been shown to be an OmpA-like protein that is largely responsible for the emulsifying activity of alasan. To further elucidate the nature of alasan, the gene coding for AlnB was cloned, sequenced and overexpressed in Escherichia coli. The overall 561 bp sequence of the hypothetical AlnB showed strong homology, including all conserved regions and residues known to be essential for enzymatic activity, to the ubiquitous family of thiol-specific antioxidant enzymes known as peroxiredoxins. Transgenic E. coli overexpressing AlnB exhibited increased resistance to cumene hydroperoxide both in liquid culture and on agar medium. Recombinant AlnB had no emulsifying activity but stabilized oil-in-water emulsion generated by AlnA.
AB - The bioemulsifier of Acinetobacter radioresistens KA53, referred to as alasan, is a high molecular weight complex of a polysaccharide and three proteins (AlnA, AlnB and AlnC). AlnA has previously been shown to be an OmpA-like protein that is largely responsible for the emulsifying activity of alasan. To further elucidate the nature of alasan, the gene coding for AlnB was cloned, sequenced and overexpressed in Escherichia coli. The overall 561 bp sequence of the hypothetical AlnB showed strong homology, including all conserved regions and residues known to be essential for enzymatic activity, to the ubiquitous family of thiol-specific antioxidant enzymes known as peroxiredoxins. Transgenic E. coli overexpressing AlnB exhibited increased resistance to cumene hydroperoxide both in liquid culture and on agar medium. Recombinant AlnB had no emulsifying activity but stabilized oil-in-water emulsion generated by AlnA.
UR - http://www.scopus.com/inward/record.url?scp=12544255531&partnerID=8YFLogxK
U2 - 10.1007/s00253-004-1712-5
DO - 10.1007/s00253-004-1712-5
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C2 - 15630518
AN - SCOPUS:12544255531
VL - 66
SP - 536
EP - 541
JO - Applied Microbiology and Biotechnology
JF - Applied Microbiology and Biotechnology
SN - 0175-7598
IS - 5
ER -