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

Endo-beta-1,4-glucanase, commonly known as cellulase, is a glycoside hydrolase enzyme that catalyzes the endohydrolysis of 1,4-beta-D-glucosidic linkages in cellulose and related polysaccharides (Ref: UniProt). Although not naturally produced by humans, it is synthesized by various bacteria, fungi, and plants, and is essential for the degradation of plant cell wall components (Ref: PubMed). In clinical medicine, the enzyme is primarily utilized as a therapeutic agent for the non-surgical dissolution of phytobezoars, which are gastric masses composed of indigestible plant fibers (Ref: Journal of Clinical Medicine). Beyond bezoar treatment, endo-beta-1,4-glucanase is increasingly investigated for its role in disrupting bacterial biofilms. Many pathogenic bacteria produce cellulose-like polymers as part of their extracellular matrix, and the application of this enzyme can degrade this matrix, increasing the susceptibility of the bacteria to antibiotics and immune clearance (Ref: ScienceDirect). Additionally, it is used as a digestive aid to assist patients with fiber malabsorption (Ref: PubChem). While generally considered safe for therapeutic use, it can act as a potent allergen in occupational settings, leading to respiratory issues such as asthma or rhinitis (Ref: NIH).

Other names

CellulaseEndoglucanase1,4-beta-D-glucan glucanohydrolasebeta-1,4-endoglucanaseCarboxymethylcellulaseAvicelase

The enzyme catalyzes the random cleavage of internal beta-1,4-D-glycosidic linkages in cellulose, lichenin, and cereal beta-D-glucans, leading to the dissolution of complex polysaccharide structures (Ref: UniProt, EC 3.2.1.4). In the treatment of phytobezoars, it breaks down the fiber-rich matrix of the gastric mass, facilitating its fragmentation and clearance (Ref: NIH StatPearls).