What is the substrate specificity of each of the Megazyme α-L-arabinofuranosidases?

Modified on Mon, 7 Nov, 2016 at 11:49 AM

The product α-L-Arabinofuranosidase (novel specificity) (Bifidobacterium adolescentis) (E-AFAM2) Data Sheet & α-L-Arabinofuranosidase B17 (Bacteroides ovatus) (E-ABFBO17) Data Sheet will remove  alpha-(1->3) linked arabinofuranosyl (Araf) at double substituted D-xylopyranosyl (dXyl). Neither of these enzymes had any action  on a-L-Araf groups singly substituted either (1-3)- or (1-2)- to Dxylosyl residues in (1-4)-b-D-xylo-oligosaccharides, whether within the xylo-oligosaccharide chain or at the non-reducing end.


α-L-Arabinofuranosidase (Ustilago maydis) (E-ABFUM) Data Sheet displays highest  activity on arabinoxylan and on a-L-Araf units (1-2)-linked [and to a lesser extent, (1-3)-linked] to a Xylp residue.


α-L-Arabinofuranosidase (Aspergillus niger) (E-AFASE) Data Sheet  displays highest  activity on A3X and rapidly hydrolysed p-nitrophenyl a-L-arabinofuranoside and (1-3)- a-L-Araf branches on sugar beet arabinan


α-L-Arabinofuranosidase B21 (Bacteroides ovatus) (E-ABFBO21) Data Sheet & α-L-Arabinofuranosidase B25 (Bacteroides ovatus) (E-ABFBO25) Data Sheet have no  action on a-L-Araf on doubly substituted Xylp residue, but rapidly hydrolyse a-L-Araf (1-3)-linked and (1-2)-linked to a Xylp residue located within a xylo-oligosaccharide chain.

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