Production and Purification of an Active endo-α-1 –> 6-D-mannanase Enzyme

At a Glance

Researchers at Colorado State University have developed successful production and purification methods of the endo-α-(1 –> 6)-D-mannanase gene from Bacillus circulans TN-31, referred to as Emn. There is currently no commercially available endo-α-(1 –> 6)-D-mannanase from any source.

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The field of glycobiology heavily relies on enzymes capable of degrading glycoconjugates to determine their structure and analyze their structure-function relationship (e.g. to study the basis of their immunogenicity or toxic properties). Despite the prevalence of glycoconjugates containing alpha-1 –> 6-linked mannoses in nature, no endo-α-(1 –> 6)-D-mannanase is commercially available.

Previously, an endo-α-(1 –> 6)-D-mannanase from Bacillus circulans proved useful in characterizing the structure of two major lipopolysaccharides of mycobacteria known as lipomannan (LM) and lipoarabinomannan (LAM). Although first reported 45 years ago, no easily accessible form of this enzyme was available to the research community, a fact that may in part be explained by lack of knowledge of its complete gene sequence.


  • Availability of this enzyme should greatly facilitate the structural analysis of α-(1–>6)-D-mannan-containing polysaccharides from any biological or synthetic source.


  • Glycobiology: Structural characterization and structure-function relationship studies involving any form of glycoconjugate (e.g. polysaccharides, lipopolysaccharides, glycoproteins, prions) containing alpha-1–>6-linked mannoses, from any biological or synthetic source (e.g., from plants, animals, prokaryotes, prion or viruses).
Last Updated: January 2024

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Mary C Jackson
Wei Li
Shiva Kumar Angala

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