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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.
The term, blend, refers to spun fibers or a fabric composed of such fibers. [1] [3] There are several synonymous terms: a combination yarn is made up of two strands of different fibers twisted together to form a ply; [1] a mixture or mixed cloth refers to blended cloths in which different types of yarns are used in warp and weft sides. [4] [5]
Compound sugars, also called disaccharides or double sugars, are molecules made of two bonded monosaccharides; common examples are sucrose (glucose + fructose), lactose (glucose + galactose), and maltose (two molecules of glucose). White sugar is a refined form of sucrose. In the body, compound sugars are hydrolysed into simple sugars.
The following other wikis use this file: Usage on af.wikipedia.org Maltose; Usage on ar.wikipedia.org مالتوز; ملتاز; Usage on ba.wikipedia.org
Amylose A is a parallel double-helix of linear chains of glucose. Amylose is made up of α(1→4) bound glucose molecules. The carbon atoms on glucose are numbered, starting at the aldehyde (C=O) carbon, so, in amylose, the 1-carbon on one glucose molecule is linked to the 4-carbon on the next glucose molecule (α(1→4) bonds). [3]
Both groups showed there were four major fractions of maltase activity that were intrinsic to two different peptide structures, sucrase-isomaltase and maltase-glucoamylase. [ 1 ] [ 2 ] [ 9 ] [ 6 ] Fifty years later entering the genomic age, cloning and sequencing of the mucosal starch hydrolase confirmed Dahlqvist and Semenza's findings.
Working from the non-reducing end, β-amylase catalyzes the hydrolysis of the second α-1,4 glycosidic bond, cleaving off two glucose units at a time. During the ripening of fruit, β-amylase breaks starch into maltose, resulting in the sweet flavor of ripe fruit. β-amylase is present in an inactive form prior to seed germination.
Maltase-glucoamylase is an alpha-glucosidase digestive enzyme. It consists of two subunits with differing substrate specificity. Recombinant enzyme studies have shown that its N-terminal catalytic domain has highest activity against maltose, while the C-terminal domain has a broader substrate specificity and activity against glucose oligomers. [7]