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A gene encoding exo-beta-(1--&gt;3)-galactanase from Irpex lacteus was cloned by reverse transcriptase-PCR. The deduced amino acid sequence showed high similarity with exo-beta-(1--&gt;3)-galactanases from other sources. The molecular mass of the mature form was calculated to be 45,520 Da. The gene product expressed in Pichia pastoris specifically hydrolyzed beta-(1--&gt;3)-galactooligosaccharides, as did other exo-beta-(1--&gt;3)-galactanases. The recombinant enzyme showed high activity toward arabinogalactan-proteins (AGPs) from radish as well as beta-(1--&gt;3)-galactan. Product analysis revealed that the enzyme released beta-(1--&gt;6)-galactobiose, beta-(1--&gt;6)-galactotriose, and alpha-L-arabinofuranosyl-(1--&gt;3)-beta-galactosyl-(1--&gt;6)-galactose together with Gal from beta-(1--&gt;3)-galactans attached with and without beta-(1--&gt;6)-galactosyl branches prepared from acacia gum. These results indicate that the exo-beta-(1--&gt;3)-galactanase from I. lacteus efficiently hydrolyzes beta-(1--&gt;3)-galactan main chains of AGPs by bypassing beta-(1--&gt;6)-galactosyl side chains.

Molecular Cloning and Expression inPichia pastorisof aIrpex lacteusExo-β-(1→3)-galactanase Gene