Researchers from UCIBIO labs (GlycoLab and XTAL) recently published a study that characterized a Carbohydrate Binding Module (CBM) from a bi-functional enzyme involved in RG-II breakdown. In the study, technologies such as X-ray crystallography, carbohydrate microarrays and microscale thermophoresis were essential for a better understanding of the function of this protein.
This new CBM shows distinctive features, such as a high content of positively charged residues and different binding signatures that set it apart from more closely related modules, which led the CAZY (Carbohydrate-Active enZymes) database to decide favourably on the creation of a new CBM family – CBM97.
The novel CBM97 family already has several putative members from other organisms from the human microbiome, which could mean the discovery of novel pectin-active proteins. Proteins with the ability to recognize pectin macromolecules specifically can have different biotechnological applications, as molecular probes for detection of pectin in plant tissues or for enhancing enzymes for industrial uses.
http://cazy.org/CBM97.html