Galactofuranosidase from JHA 19 Streptomyces sp:. subcloning and biochemical characterization

Abstract : Despite the crucial role of the rare galactofuranose (Galf) in many pathogenic micro-organisms and our increased knowledge of its metabolism, there is still a lack of recombinant and efficient galactofuranoside hydrolase available for chemo-enzymatic synthetic purposes of specific galactofuranosyl-conjugates. Subcloning of the Galf-ase from JHA 19 Streptomyces sp. and its further overexpression lead us to the production of this enzyme with a yield of 0.5 mg/L of culture. It exhibits substrate specificity exclusively towards pNP beta-D-Galf, giving a K-M value of 250 mu M, and the highest enzymatic efficiency ever observed of 14 mM(-1) s(-1). It proved to be stable to temperature up to 60 degrees C and to at least 4 freeze-thaw's cycles. Thus, Galf-ase demonstrated to be an efficient and stable biocatalyst with greatly improved specificity toward the galactofuranosyl entity, thus paving the way to the further development of transglycosylation and thioligation reactions.
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Mateja Senicar, Laurent Legentil, Vincent Ferrières, Svetlana Eliseeva, Stéphane Petoud, et al.. Galactofuranosidase from JHA 19 Streptomyces sp:. subcloning and biochemical characterization. Carbohydrate Research, Elsevier, 2019, 480, pp.35-41. ⟨10.1016/j.carres.2019.05.011⟩. ⟨hal-02177806⟩

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