An arabinoxylan de-branching enzyme can be modified to gain backbone cleaving activity.

What is it about?

The crystal structure and full biochemical characterisation are presented for a glycoside hydrolase that removes a very specific arabinose decoration from arabinoxylan, with high specificity. We show that simple mutagenesis of one surface amino acid close to the active site introduces the capacity for cleavage of the xylan backbone, while retaining the wild-type specificity.

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Why is it important?

The costs and energy requirements of enzyme production are one major bottleneck in commercial lignocellulose breakdown in a sustainable biorefinery. The possibility of using fewer enzymes with multiple activities is attractive for this reason.