Characterization of an endo-processive-type xyloglucanase having a β-1,4-glucan-binding module and an endo-type xyloglucanase from Streptomyces avermitilis.

@article{Ichinose2012CharacterizationOA,
  title={Characterization of an endo-processive-type xyloglucanase having a β-1,4-glucan-binding module and an endo-type xyloglucanase from Streptomyces avermitilis.},
  author={Hitomi Ichinose and Yuko Araki and Mari Michikawa and Koichi Harazono and Katsuro Yaoi and Shuichi Karita and Satoshi Kaneko},
  journal={Applied and environmental microbiology},
  year={2012},
  volume={78 22},
  pages={7939-45}
}
We cloned two glycoside hydrolase family 74 genes, the sav_1856 gene and the sav_2574 gene, from Streptomyces avermitilis NBRC14893 and characterized the resultant recombinant proteins. The sav_1856 gene product (SaGH74A) consisted of a catalytic domain and a family 2 carbohydrate-binding module at the C terminus, while the sav_2574 gene product (SaGH74B) consisted of only a catalytic domain. SaGH74A and SaGH74B were expressed successfully and had molecular masses of 92 and 78 kDa, respectively… CONTINUE READING
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