Lactobacillus plantarum WCFS1 β-Fructosidase: Evidence for an Open Funnel-Like Channel Through the Catalytic Domain with Importance for the Substrate Selectivity

@article{MendozaLlerenas2016LactobacillusPW,
  title={Lactobacillus plantarum WCFS1 $\beta$-Fructosidase: Evidence for an Open Funnel-Like Channel Through the Catalytic Domain with Importance for the Substrate Selectivity},
  author={Edgar Omar Mendoza-Llerenas and David J. P{\'e}rez and Zeferino G{\'o}mez-Sandoval and Pilar Escalante-Minakata and Vrani Ibarra-Junquera and Rodrigo Said Razo‐Hern{\'a}ndez and Vittorio Capozzi and Pasquale Russo and Giuseppe Spano and Daniela Fiocco and Juan A. Osuna‐Castro and Abel Moreno},
  journal={Applied Biochemistry and Biotechnology},
  year={2016},
  volume={180},
  pages={1056-1075}
}
Abstractβ-Fructosidase, a glycoside hydrolase of a biotechnologically important strain, was studied for its biochemical, physicochemical, and three-dimensional structure characteristics. This enzyme was heterologously expressed in Escherichia coli as a C-terminal His-tagged protein (SacB). β-Fructosidase catalyzes the cleavage of glycoside bonds toward certain carbohydrates with β-fructofuranosyl linkages; however, SacB exhibited selectivity toward sucrose and an optimum activity at pH 6.0–6.5… 
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