Novel Enzyme for hydrolysing glucuronoxyla to improv the yield from pulp material

Novel Enzyme for hydrolysing glucuronoxyla to improv the yield from pulp material

Technology Description

Currently during the pulping process, hemicelluloses such as xylan don’t form tightly packed crystalline structures compared to celluloses because of complex structural side chains. Alkaline cooking liquors of the pulping process degrade potentially high value hemicelluloses and their by-products as a result of the hash processing and resulting in a loss of yield from the pulp material.

Hemicelluloses are valuable in the process because they are thought to contribute to the swelling of the pulp and therefore the conformation of the fibres during sheet formation. This value is lost due to the degradation of xylan in the pulping process. 

We have isolated an alph-glucoronidase with the ability of degrading a glycosidic linkage between a MeGlcA residue and a non-terminal xylopyranosyl residue from glucuronoxylan obtained from various plant biomasses in order to minimize the loss of xylans.

Current enzymes used in this process are limited because they liberate MeGlcA or GlcA only from fragments of glucuronoxylan where the uronic acid is linked to the non-reducing terminal.



Target Industries

Plant biomass processing industries, paper pulping companies

Unique Features/Benefits

The alpha-glucuronidase is capable of selectively processing the complex hemicelluloses xylan side-chains in the pulping process. One of the benefits of our isolated alpha-glucuronosidase is that it cleaves glycosidic side linkages within polymeric substrates such as glucuronoxylan.

Innovation Status

A national phase application has been filed.


The enzyme technology can be demonstrated at lab scale.

Principal Researchers

VAN ZYL, Willem Heber

BIELY, Peter


CHIMPHANGO, Annie Fabian Abel

GöRGENS, Johann Ferdinand

Available for licensing



Ian van Zyl