The enzymatic degradation and modification of hemicelluloses, important components of lignocellulosic biomass, holds great potential for creating renewable alternatives to fossil-based products. One of the enzyme types responsible for this is �-mannanases, which are glycoside hydrolases (GHs) and catalyze hydrolysis of �-1,4-mannosidic bonds in the backbone of mannan-based hemicelluloses. They are found in the GH5, GH26 and GH113 enzyme families. Using �-mannanases in conjunction with other enzymes could enable more efficient degradation of lignocellulosic biomass and give higher yield for subsequent applications. Some �-mannanases are also able to perform transglycosylation, i.e. synthesize new �-mannosidic bonds, or transfer other molecules, e.g. alcohols, onto mannooligosaccharides. Since it has proven to be very difficult to synthesize the �-mannosidic bond chemically, this type of enzymatic synthesis is valuable. However, significant differences exist between �-mannanases in substrate binding, specificity, and conversion efficiency. In order to understand their structure-function relationships, characterization of �-mannanases from various organisms is therefore essential. Research from our group has shown that specific residues in the active sites of �-mannanases are important determinants of substrate binding, specificity and transfer capacity, and that substituting these residues can alter the properties of the enzymes. We will describe our work on �-mannanases from a variety of organisms, including the filamentous fungus Trichoderma reesei and the blue mussel Mytilus edulis, and their applicability in mannan-based hemicellulose modification.

Structure and function of �-mannanases from microbes and the blue mussel

247th National Meeting (2014)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.