Abstract
In this study we demonstrate that the abp gene in Geobacillus stearothermophilus T-6 encodes a family 27 glycoside hydrolase β-l-arabinopyranosidase. The catalytic constants towards the chromogenic substrate pNP-β-l-arabinopyranoside were 0.8±0.1mM, 6.6±0.3s−1, and 8.2±0.3s−1mM−1 for Km, kcat and kcat/Km, respectively. 13C NMR spectroscopy unequivocally showed that Abp is capable of removing β-l-arabinopyranose residues from the natural arabino-polysaccharide, larch arabinogalactan. Most family 27 enzymes are active on galactose and contain a conserved Asp residue, whereas in Abp this residue is Ile67, which shifts the specificity of the enzyme towards arabinopyranoside.
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