There are a number of different enzymes necessary for the microbial degradation of cellulose and xylan, including endocrine glucanases, cellulose biohydrolases (exoglucanases), and xylanases. Different types of cellulose-degrading enzymes (cellulases) and xylanases are produced by different types of fungi and bacteria, and these enzymes can be categorized into families based on their shared amino acid sequence. Enzymes belonging to the glycosyl hydrolase family break down glycosidic bonds, which connect two or more sugars or a sugar and a non-sugar molecule. Classification schemes for glycosyl hydrolases based on sequence similarity have identified 85 distinct families. Aamy is an alpha-amylase domain. Glycosyl hydrolase family 13 includes enzymes like alpha-amylases because they contain this domain. Catalyzed hydrolysis of (1-4)-D-glycosidic bonds in polysaccharides is the process by which maltogenic-amylase transforms starch into maltose. IPR010502 encodes a carbohydrate-binding domain of the family 9 (CBD9). Enzymes that break down cellulose and xylan have a part called CBD9 that binds to cellulose, xylan, and a number of soluble disaccharides and monosaccharides. PA14 (IPR037524) can be found in a wide range of proteins in bacteria and eukaryotes, including glycosidases, glycosyltransferases, proteases, amidases, toxins, adhesins, and signaling molecules. In a mosaic-like way, the PA14 domain interacts with other domains, both catalytic and non-catalytic, that are involved in carbohydrate and peptidoglycan binding. Both eukaryotes and prokaryotes rely on glycoside hydrolases (GHs) for crucial processes, such as the acquisition of substrates, the long-range remodeling of cell walls, and the glycan modification of glycoproteins. Among the enzymes that share the glycoside hydrolase family 10 domain (IPR001000, GH10) are xylanases, endo-1,3-beta-xylanases, and cellulose biohydrolases, also known as cellulases family F. All of the enzymes in the glycosyl hydrolase family 16 (GH16) are descended from a common ancestor but have diverged greatly in primary sequence. Chitinase and endo-N-acetyl-D-glucosaminidase (ENGase) hydrolases, as well as a chitinase-like lectin (capsicum lectin), are all members of the glycosyl hydrolase family 18 (GH18). Chitinases are hydrolases that release 1,4-linkages by cleaving oligomeric, dimeric, or monomeric chitin. In order to remove N-linked glycans from glycoproteins, ENGases hydrolyze the-1,4 bond in the chitobiose core, which leaves a GlcNAc residue. Most members of GH26 are 1,4-mannanases (mannanases) found in the body, but some also have 1,3-xylanase activity. Endoglucanase H, which catalyzes the endohydrolysis of 1,4-beta-glucuronide linkages in cellulose, lichenin, and grain beta-D-glucans, is also one of the proteins that contain this domain.