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

Seničar, Mateja; Legentil, Laurent; Ferrières, Vincent; Eliseeva, Svetlana V.; Petoud, Stéphane; Takegawa, Kaoru; Lafite, Pierre; Daniellou, Richard

doi:10.1016/j.carres.2019.05.011

Cited by 6 publications

(3 citation statements)

References 31 publications

(29 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…XynD displays an optimum pH between pH 4 and pH 5, and concurs with previously described recombinant galacto-furanosidases with varying optimum pHs of 3-7 28,30,34,49,50 . Optimal temperature of characterized galactofuranosidases vary, for example, the Galf-ase derived from Streptomyces sp.…”

Section: Discussionsupporting

confidence: 88%

See 1 more Smart Citation

Biochemical characterization of a glycoside hydrolase family 43 β-D-galactofuranosidase from the fungus Aspergillus niger

Yuen

Begum

et al. 2021

Preprint

View full text Add to dashboard Cite

Abstractβ-D-Galactofuranose (Galf) and its polysaccharides are found in bacteria, fungi and protozoa but do not occur in mammalian tissues, and thus represent a specific target for anti-pathogenic drugs. Understanding the enzymatic degradation of these polysaccharides is therefore of great interest, but the identity of fungal enzymes with exclusively galactofuranosidase activity has so far remained elusive. Here we describe the identification and characterization of a galactofuranosidase from the industrially important fungus Aspergillus niger. Phylogenetic analysis of glycoside hydrolase family 43 subfamily 34 (GH43_34) members revealed the occurrence of three distinct clusters and, by comparison with specificities of characterized bacterial members, suggested a basis for prediction of enzyme specificity. Using this rationale, in tandem with molecular docking, we identified a putative β-D-galactofuranosidase from A. niger which was recombinantly expressed in Escherichia coli. The Galf-specific hydrolase, encoded by xynD demonstrates maximum activity at pH 5, 25 °C towards 4-Nitrophenyl-β-galactofuranoside (pNP-β-Galf), with a Km of 17.9 ± 1.9 mM and Vmax of 70.6 ± 5.3 μmol min−1. The characterization of this first fungal GH43 galactofuranosidase offers further molecular insight into the degradation of Galf-containing structures and may inform clinical treatments against fungal pathogens.

show abstract

Section: Discussionsupporting

confidence: 88%

“…JHA26 lost its activity when incubated at a temperature over 45 °C whilst Streptomyces sp. JHA19 galactofuranosidases had an optimal temperature at 60 °C 50,51 . Since XynD was expressed in E. coli no post translational modifications, such as glycosylation, will have occurred.…”

Section: Discussionmentioning

confidence: 99%