Search results
Results from the WOW.Com Content Network
In humans, maltose is broken down by various maltase enzymes, providing two glucose molecules that can be further processed: either broken down to provide energy, or stored as glycogen. The lack of the sucrase-isomaltase enzyme in humans causes sucrose intolerance , but complete maltose intolerance is extremely rare because there are four ...
Sucrose intolerance or genetic sucrase-isomaltase deficiency (GSID) is the condition in which sucrase-isomaltase, an enzyme needed for proper metabolism of sucrose (sugar) and starch (e.g., grains), is not produced or the enzyme produced is either partially functional or non-functional in the small intestine.
Maltose Ligand (NAG) interactions in Maltase-Glucoamylase Interactions of oligosaccharides in Alpha-amylase. Maltase is an informal name for a family of enzymes that catalyze the hydrolysis of disaccharide maltose into two simple sugars of glucose. Maltases are found in plants, bacteria, yeast, humans, and other vertebrates.
Maltitol is a disaccharide produced by hydrogenation of maltose obtained from starch. Maltitol syrup, a hydrogenated starch hydrolysate, is produced by hydrogenating corn syrup, a mixture of carbohydrates produced from the hydrolysis of starch. This product contains between 50% and 80% maltitol by weight.
It causes the sexually transmitted genitourinary infection gonorrhea [6] as well as other forms of gonococcal disease including disseminated gonococcemia, septic arthritis, and gonococcal ophthalmia neonatorum. N. gonorrhoeae is oxidase positive and a microaerophile that is capable of surviving phagocytosis and growing inside neutrophils. [6]
Staphylococcus xylosus is a species of bacteria belonging to the genus Staphylococcus.It is a Gram-positive bacterium that forms clusters of cells. Like most staphylococcal species, it is coagulase-negative and exists as a commensal on the skin of humans and animals and in the environment.
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]
When eaten by humans, isomaltulose is digested completely and absorbed. [9] Its intestinal digestion involves the enzyme isomaltase, which is located at the surface of the brush border lining the inner wall of the small intestine. This enzyme is otherwise involved in the digestion of α-1,6 linkages present in starch.