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Maltose (/ ˈ m ɔː l t oʊ s / [2] or / ˈ m ɔː l t oʊ z / [3]), also known as maltobiose or malt sugar, is a disaccharide formed from two units of glucose joined with an α(1→4) bond. In the isomer isomaltose , the two glucose molecules are joined with an α(1→6) bond.
A glycosidic bond or glycosidic linkage is a type of ether bond that joins a carbohydrate (sugar) molecule to another group, which may or may not be another carbohydrate. Formation of ethyl glucoside: Glucose and ethanol combine to form ethyl glucoside and water .
A disaccharide (also called a double sugar or biose) [1] is the sugar formed when two monosaccharides are joined by glycosidic linkage. [2] Like monosaccharides, disaccharides are simple sugars soluble in water. Three common examples are sucrose, lactose, and maltose.
Beta-amylase is found in bacteria, fungi, and plants; bacteria and cereal sources are the most heat stable. Working from the non-reducing end, β-amylase catalyzes the hydrolysis of the second α-1,4 glycosidic bond, cleaving off two glucose units ( maltose ) at a time.
Beta-amylase [8] [9] is an enzyme that hydrolyzes 1,4-alpha-glucosidic linkages in starch-type polysaccharide substrates so as to remove successive maltose units from the non-reducing ends of the chains. Beta-amylase is present in certain bacteria as well as in plants. Three highly conserved sequence regions are found in all known beta-amylases.
α-Amylase is an enzyme (EC 3.2.1.1; systematic name 4-α-D-glucan glucanohydrolase) that hydrolyses α bonds of large, α-linked polysaccharides, such as starch and glycogen, yielding shorter chains thereof, dextrins, and maltose, through the following biochemical process: [2]
The starch is first converted, by means of simple enzymatic hydrolysis, into high maltose syrup with di-, tri and oligosaccharides (2, 3 or more glucose units) having α(1,4)-glycosidic linkages which are readily digestible in the human intestine. These α(1,4)-glycosidic linkages are further converted into digestion-resistant α(1,6 ...
Hydrolysis reaction of Maltose being broken at the 1-4 alpha-glucosidase linkage. The mechanism of all FamilyGH13 enzymes is to break a α-glucosidase linkage by hydrolyzing it. Maltase focuses on breaking apart maltose, a disaccharide that is a link between 2 units of glucose, at the α-(1->4) bond.