β-Glucosidase (; systematic name β-D-glucoside glucohydrolase) is an enzyme that catalyses the following reaction: Hydrolysis of terminal, non-reducing β-D-glucosyl residues with release of β-D-glucose
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β-Glucosidase (; systematic name β-D-glucoside glucohydrolase) is an enzyme that catalyses the following reaction: Hydrolysis of terminal, non-reducing β-D-glucosyl residues with release of β-D-glucose
== Structure == β-Glucosidase is composed of two polypeptide chains. Each chain is made up of 438 amino acids and constitute a subunit of the enzyme. Each of these subunits contains an active site. The active site has three potential components: the pocket, the cleft, and the tunnel. The pocket structure is beneficial for recognition of monosaccharide like glucose. The cleft allows for binding of sugars to form polysaccharides. The tunnel allows for the enzyme to attach to polysaccharide and then release product while still attached to the sugar.
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