The enzyme, which was characterized from dormant seeds of the plant?Cajanus cajan?(pigeon pea), has been shown to remove the terminal non-reducing ¦Â-L-arabinopyranoside residue from the artificial substrate?p-nitrophenyl-¦Â-L-arabinopyranose [1]. In the presence of methanol the enzyme demonstrates transglycosylase activity, transferring the arabinose moiety to methanol while retaining the anomeric configuration, generating 1-O-methyl-¦Â-L-arabinopyranose [2].
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Removal of a terminal beta-L-arabinopyranose residue from the non- reducing end of its substrate.
