Endo-1,4-beta-glucanase (EG)

Endo-1,4-beta-glucanase, frequently referred to as cellulase, is an enzyme responsible for the internal cleavage of beta-1,4-glycosidic bonds in cellulose and other beta-glucan chains (UniProt EC 3.2.1.4). Although humans do not endogenously produce this enzyme, it is widely synthesized by bacteria, fungi, and plants for the degradation of structural polysaccharides (PubMed PMID: 30251177). In clinical practice, these enzymes are often included in multi-enzyme digestive supplements to aid in the breakdown of plant-based fibers, potentially benefiting patients with malabsorption syndromes or general digestive insufficiency (PubChem CID 131751471). Beyond digestion, endo-1,4-beta-glucanases are being explored as therapeutic agents to disrupt the extracellular matrix of bacterial biofilms, particularly in chronic infections like those caused by Pseudomonas aeruginosa, thereby increasing the efficacy of co-administered antibiotics (PubMed PMID: 28844936). The enzyme's interaction with drugs is primarily characterized by its use as a therapeutic protein or its inhibition by small molecules like cellobiose in industrial or research settings. Safety considerations include potential allergic reactions, especially when the enzyme is derived from fungal sources such as Aspergillus or Trichoderma.

Other names

CellulaseEndocellulase1,4-beta-D-glucan 4-glucanohydrolaseBeta-1,4-glucanaseCarboxymethylcellulase

Hydrolysis of internal beta-1,4-D-glucosidic linkages in cellulose and cereal beta-D-glucans; as a therapeutic, it facilitates the breakdown of dietary fiber or disrupts bacterial biofilm matrices.