Maltase Enzyme

Introduction to Maltase

Maltase (EC 3.2.1.20, alpha-glucosidase, glucoinvertase, glucosidosucrase, maltase-glucoamylase, alpha-glucopyranosidase, glucosidoinvertase, alpha-D-glucosidase, alpha-glucoside hydrolase, alpha-1,4-glucosidase, alpha-D-glucoside glucohydrolase) is a type of alpha-glucosidase enzyme found in the small intestine’s brush border.

This enzyme catalyses the hydrolysis of the disaccharide maltose into two simple glucose sugars. Plants, bacteria, yeast, humans, and other vertebrates have maltase. It is supposed to be made by cells in the mucous membrane that lines the inside of the intestine.

Table of Contents

• Structure and Mechanism of Maltase
• Maltase Enzyme Production
• Intestinal Enzymes and Industrial Applications
• Deficiency of Maltase
• Maltose versus Maltase
• Frequently Asked Questions – FAQs

Structure and Mechanism of Maltase

Structure of Maltase Enzyme

Maltase belongs to the GH13 (Glycoside hydrolase family 13) group of intestinal enzymes that convert complex carbohydrates’ glucosidase connections into simple glucose molecules for consumption. The glucose molecules would then be used as a kind of “meal” for cells in order to manufacture energy (Adenosine triphosphate) during cellular respiration. Maltase can be coded for by the genes listed below:

• The GAA gene codes for acid alpha-glucosidase, which is required for the breakdown of complex sugars termed Glycogen into glucose.
• Maltase-glucoamylase, which is encoded by the MGAM gene, is involved in starch digestion. In humans, this enzyme is responsible for the digestion of plant-based carbohydrates.
• Sucrase-isomaltase is required for the digestion of carbohydrates such as starch, sucrose, and isomaltose, and is encoded by the SI gene.
• The AMY1A gene codes for alpha-amylase 1, which is responsible for cleaving -glucosidase links in oligosaccharides and polysaccharides to produce starches and glycogen for the previous enzymes to catalyse. The presence of more of this gene in the brain has been linked to a lower risk of Alzheimer’s disease.

Mechanism of Maltase

The mechanism of all Family GH13 enzymes is the hydrolysis of alpha-glucosidase linkage. Maltase is a disaccharide having a -(1->4) link connecting two glucose units that are used to dissolve maltose. The rate of hydrolysis is determined by the size of the substrate (or the carbohydrate size).

Further Reading:

What is Maltose?

Maltase Enzyme Production

During digestion, salivary or pancreatic enzymes known as amylases (amylase maltase) partially convert starch to maltose; maltase is released by the colon and then transforms maltose to glucose. The glucose produced is either used by the organism or stored as glycogen in the liver (animal starch).

Intestinal Enzymes and Industrial Applications

Starch digestion requires six intestinal enzymes, two of which are luminal endo-glucosidases, commonly known as alpha-amylases. The remaining four enzymes have been identified as maltases and exo-glucosidases bound to the luminal surface of enterocytes.

These maltase activities were connected to the sucrase-isomaltase system (maltase Ib, maltase Ia). Maltase-glucoamylase was given to the other two maltases with no differentiating properties (also called maltases II and III). These four maltases are alpha-glucosidase because they all digest linear starch oligosaccharides to glucose.

In some aspects, it’s similar to alpha-glucosidase, but “maltase” stresses the substrate’s disaccharide character, where the glucose is cleaved, whereas “alpha-glucosidase” focuses the link whether the substrate is polysaccharide or disaccharide.

Industrial Applications

Because alpha-amylase plays a crucial role in breaking starches, it is widely employed in the baking business. It’s generally used as a taste enhancer to improve bread quality. Yeast would be unable to ferment without alpha-amylase.

Maltose-glucoamylase is commonly used as a fermentation source because it can break starch into maltose, which can then be used to make sake and beers.

Outside of brewing, maltose glucoamylase has been explored by adding complex inhibitors to prevent the hydrolysis of alpha-glucosidase connections. Scientists want to develop a less harmful medication and more effective for treating diabetes by inhibiting the linkage cleave.

Deficiency of Maltase

In 1932, Dutch pathologist JC Pompe originally described acid maltase deficiency (AMD), better known as Pompe disease. AMD is a non-sex related autosomal recessive disorder in which lysosome vacuoles in practically all types of cells throughout the body accumulate excessive glycogen. It is one of the most dangerous glycogen storage illnesses that affects muscular tissue.

AMD is divided into three kinds according to the age at which symptoms first appear in affected individuals. Types a, b, and c describe infantile, childhood, and adulthood. The gene mutation type found at 17q23 determines the type of AMD. At the same time, the kind of mutation determines how much acid maltase is produced.

AMD is lethal, and type-a children usually die of heart failure before they reach the age of one. Type-b children die of respiratory failure between the ages of 3 and 24. Type-c patients die of respiratory failure between the ages of 10 and 20 years after symptoms.

Maltose versus Maltase

Main differences between maltose and maltase are as follows: