Molecular and biochemical characterizations of a novel arthropod endo-beta-1,3-glucanase from the Antarctic springtail, Cryptopygus antarcticus, horizontally acquired from bacteria.

@article{Song2010MolecularAB,
  title={Molecular and biochemical characterizations of a novel arthropod endo-beta-1,3-glucanase from the Antarctic springtail, Cryptopygus antarcticus, horizontally acquired from bacteria.},
  author={Jung Min Song and Kiwoong Nam and Young-Uk Sun and Mee Hye Kang and Choong-gon Kim and S -C Kwon and Jehee Lee and Youn-Ho Lee},
  journal={Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology},
  year={2010},
  volume={155 4},
  pages={
          403-12
        }
}
Collembolan species have been known to have beta-1,3-glucanase activity and yet the genes coding such enzymes have not been demonstrated. We report here a novel arthropod endo-beta-1,3-glucanase gene CaLam from the Antarctic springtail, Cryptopygus antarcticus. The open reading frame consists of 813bp encoding 270 amino acids with a putative signal peptide and a typical motif of glycosyl hydrolase family 16 (GHF16), E-I-D-I-T-E. The recombinant protein expressed in E. coli shows the hydrolytic… CONTINUE READING