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A disaccharide is the sugar formed when two monosaccharides are joined by glycosidic linkage. Like monosaccharides, disaccharides are simple sugars soluble in water. Three common examples are sucrose, lactose, and maltose.
Hydrolysis is any chemical reaction in which a molecule of water breaks one or more chemical bonds. The term is used broadly for substitution, elimination, and solvation reactions in which water is the nucleophile.
Lactase is an enzyme produced by many organisms and is essential to the complete digestion of whole milk. It breaks down the sugar lactose into its component parts, galactose and glucose. Lactase is found in the brush border of the small intestine of humans and other mammals. People deficient in lactase or lacking functional lactase may experience the symptoms of lactose intolerance after consuming milk products. Lactase can be purchased as a food supplement and is added to milk to produce "lactose-free" milk products.
An amylase is an enzyme that catalyses the hydrolysis of starch into sugars. Amylase is present in the saliva of humans and some other mammals, where it begins the chemical process of digestion. Foods that contain large amounts of starch but little sugar, such as rice and potatoes, may acquire a slightly sweet taste as they are chewed because amylase degrades some of their starch into sugar. The pancreas and salivary gland make amylase to hydrolyse dietary starch into disaccharides and trisaccharides which are converted by other enzymes to glucose to supply the body with energy. Plants and some bacteria also produce amylase. Specific amylase proteins are designated by different Greek letters. All amylases are glycoside hydrolases and act on α-1,4-glycosidic bonds.
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.
Maltase is one type of alpha-glucosidase enzymes located in the brush border of the small intestine. This enzyme catalyzes the hydrolysis of disaccharide maltose into two simple sugars of glucose. Maltase is found in plants, bacteria, yeast, humans, and other vertebrates. It is thought to be synthesized by cells of the mucous membrane lining the intestinal wall.
Inverted sugar syrup, also called invert syrup, invert sugar, simple syrup, sugar syrup, sugar water, bar syrup, syrup USP, or sucrose inversion, is a syrup mixture of the monosaccharides glucose and fructose, that is made by hydrolytic saccharification of the disaccharide sucrose. This mixture's optical rotation is opposite to that of the original sugar, which is why it is called an invert sugar.
In chemistry, a glycoside is a molecule in which a sugar is bound to another functional group via a glycosidic bond. Glycosides play numerous important roles in living organisms. Many plants store chemicals in the form of inactive glycosides. These can be activated by enzyme hydrolysis, which causes the sugar part to be broken off, making the chemical available for use. Many such plant glycosides are used as medications. Several species of Heliconius butterfly are capable of incorporating these plant compounds as a form of chemical defense against predators. In animals and humans, poisons are often bound to sugar molecules as part of their elimination from the body.
In biochemistry, hydrolases constitute a class of enzymes that commonly function as biochemical catalysts that use water to break a chemical bond:
Acarbose (INN) is an anti-diabetic drug used to treat diabetes mellitus type 2 and, in some countries, prediabetes. It is a generic sold in Europe and China as Glucobay, in North America as Precose, and in Canada as Prandase.
The enzyme Trehalase is a glycoside hydrolase, produced by cells in the brush border of the small intestine, which catalyzes the conversion of trehalose to glucose. It is found in most animals.
Disaccharidases are glycoside hydrolases, enzymes that break down certain types of sugars called disaccharides into simpler sugars called monosaccharides. In the human body, disaccharidases are made mostly in an area of the small intestine's wall called the brush border, making them members of the group of "brush border enzymes".
β-Glucosidase is an enzyme that catalyses the following reaction:
α-Glucosidase (EC 3.2.1.20, is a glucosidase located in the brush border of the small intestine that acts upon α bonds:
The term glycosynthase refers to a class of proteins that have been engineered to catalyze the formation of a glycosidic bond. Glycosynthase are derived from glycosidase enzymes, which catalyze the hydrolysis of glycosidic bonds. They were traditionally formed from retaining glycosidase by mutating the active site nucleophilic amino acid to a small non-nucleophilic amino acid. More modern approaches use directed evolution to screen for amino acid substitutions that enhance glycosynthase activity.
In biochemistry, glycoside hydrolases are a class of enzymes which catalyze the hydrolysis of glycosidic bonds in complex sugars. They are extremely common enzymes, with roles in nature including degradation of biomass such as cellulose (cellulase), hemicellulose, and starch (amylase), in anti-bacterial defense strategies, in pathogenesis mechanisms and in normal cellular function. Together with glycosyltransferases, glycosidases form the major catalytic machinery for the synthesis and breakage of glycosidic bonds.
Glucan 1,4-α-glucosidase is an enzyme located on the brush border of the small intestine with systematic name 4-α-D-glucan glucohydrolase. It catalyses the following chemical reaction
In molecular biology, glycoside hydrolase family 68 is a family of glycoside hydrolases.
In molecular biology, glycoside hydrolase family 27 is a family of glycoside hydrolases.
Glucanases are enzymes that break down large polysaccharides via hydrolysis. The product of the hydrolysis reaction is called a glucan, a linear polysaccharide made of up to 1200 glucose monomers, held together with glycosidic bonds. Glucans are abundant in the endosperm cell walls of cereals such as barley, rye, sorghum, rice, and wheat. Glucanases are also referred to as lichenases, hydrolases, glycosidases, glycosyl hydrolases, and/or laminarinases. Many types of glucanases share similar amino acid sequences but vastly different substrates. Of the known endo-glucanases, 1,3-1,4-β-glucanase is considered the most active.
References
- ↑ "Definition of SACCHARIFICATION". www.merriam-webster.com.
- ↑ "Definition of Saccharification". www.merriam-webster.com. Archived from the original on 7 January 2021. Retrieved 8 September 2020.
- ↑ Bowen, Richard. "Small Intestinal Brush Border Enzymes". VIVO Pathophysiology. Retrieved 30 November 2019.
- ↑ Woo, K. S.; Kim, H. Y.; Hwang, I. G.; Lee, S. H.; Jeong, H. S. (2015). "Characteristics of the Thermal Degradation of Glucose and Maltose Solutions". Prev Nutr Food Sci. 20 (2): 102–9. doi:10.3746/pnf.2015.20.2.102. PMC 4500512 . PMID 26175997.
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