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In the absence of naturally available galactofuranose-specific lectin, we report herein the bioengineering of Gal<i>f</i>NeoLect, from the first cloned wild-type galactofuranosidase (<i>Streptomyces</i> sp. strain JHA19), which recognises and binds a single monosaccharide that is only related to nonmammalian species, usually pathogenic microorganisms. We kinetically characterised the Gal<i>f</i>NeoLect to confirm attenuation of hydrolytic activity and used competitive inhibition assay, with close structural analogues of Gal<i>f</i>, to show that it conserved interaction with its original substrate. We synthetised the bovine serum albumin-based neoglycoprotein (Gal<i>f</i>NGP), carrying the multivalent Gal<i>f</i> units, as a suitable ligand and high-avidity system for the recognition of Gal<i>f</i>NeoLect which we successfully tested directly with the galactomannan spores of <i>Aspergillus brasiliensis</i> (ATCC 16404). Altogether, our results indicate that Gal<i>f</i>NeoLect has the necessary versatility and plasticity to be used in both research and diagnostic lectin-based applications.