Biochemical properties and substrate specificities of a recombinantly produced Azotobacter vinelandii alginate lyase.

@article{Ertesvg1998BiochemicalPA,
  title={Biochemical properties and substrate specificities of a recombinantly produced Azotobacter vinelandii alginate lyase.},
  author={Helga Ertesv{\aa}g and F Erlien and Gudmund Skj{\aa}k-Braek and Bernd H A Rehm and Svein Valla},
  journal={Journal of bacteriology},
  year={1998},
  volume={180 15},
  pages={3779-84}
}
Alginate is a polysaccharide composed of beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G). An Azotobacter vinelandii alginate lyase gene, algL, was cloned, sequenced, and expressed in Escherichia coli. The deduced molecular mass of the corresponding protein is 41.4 kDa, but a signal peptide is cleaved off, leaving a mature protein of 39 kDa. Sixty-three percent of the amino acids in this mature protein are identical to those in AlgL from Pseudomonas aeruginosa. AlgL was partially… CONTINUE READING

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