Glycoside Hydrolase Applications in Biomass Degradation

Glycoside hydrolases constitute a vast class of enzymes that catalyse the hydrolysis of glycosidic bonds in complex polysaccharides, thereby playing a central role in the conversion of plant and algal biomass into valuable sugars and oligosaccharides. These enzymes often carry one or more carbohydrate-binding modules (CBMs) that enhance substrate recognition and binding, thereby boosting catalytic efficiency. In lignocellulosic feedstocks, ensembles of endoglucanases, exoglucanases and accessory enzymes synergise to depolymerise cellulose and hemicellulose, facilitating subsequent fermentation into biofuels or platform chemicals. In marine systems, specific β-1,3-glucanases target algal storage polysaccharides such as laminarin, unlocking new routes to renewable bioproducts. Recent advances in structural biology have revealed the molecular basis of substrate specificity, thermostability and cold-adaptation, guiding rational engineering of enzyme variants with improved performance under industrial conditions. Enzyme cocktails, informed by sequence-function mapping and subfamily classification within major glycoside hydrolase families, now enable tailored degradation of diverse biomass sources, from agricultural residues to marine polymers. These developments underpin sustainable strategies for carbon recycling and the production of high-value oligosaccharides, advancing both bioenergy and bioproduct sectors.

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Glycoside Hydrolase Applications in Biomass Degradation publication trend

The graph below shows the total number of articles in glycoside hydrolase applications in biomass degradation across all publications each year (not limited to Nature Index journals).

Technical terms

Glycoside hydrolase: Enzyme that cleaves glycosidic bonds in carbohydrates, enabling polysaccharide depolymerisation.

Carbohydrate-binding module (CBM): Non-catalytic domain that recognises and binds specific polysaccharide structures, enhancing enzyme–substrate affinity.

Endoglucanase: Enzyme that hydrolyses internal bonds within glucan chains, generating oligosaccharides of varying length.

Lignocellulose: Composite plant biomass material composed of cellulose, hemicellulose and lignin, resistant to enzymatic degradation without pretreatment.

References

1. Structural insights into curdlan degradation via a glycoside hydrolase containing a disruptive carbohydrate-binding module. Biotechnology for Biofuels and Bioproducts (2024).
2. Novel, cold-adapted D-laminaribiose- and D-glucose-releasing GH16 endo-β-1,3-glucanase from Hymenobacter siberiensis PAMC 29290, a psychrotolerant bacterium from Arctic marine sediment. Frontiers in Microbiology (2024).
3. Unveiling the role of novel carbohydrate‐binding modules in laminarin interaction of multimodular proteins from marine Bacteroidota during phytoplankton blooms. Environmental Microbiology (2024).