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How is maltase affected by temperature? These results suggested that maltase can with stand 40 °C and 45 °C for longer time intervals as compared to other temperatures. The loss of maltase activity at high temperatures due to exposure for longer time might be due to the increase in kinetic energy of the molecules.
Does maltase require high temperature? Some properties of the partially purified maltase were determined: optimum pH, 6.5; optimum temperature, 48 to 50°C; pH stability range, 5.0 to 7.0; temperature stability range, 0 to 50°C; isoelectric point, pH 5.2; and molecular weight, 52,000.
Why does maltase work at body temperature? Maltose is hydrolysed by the enzyme maltase. In humans, the enzyme maltase breaks down maltose to glucose. This takes place at normal body temperature.
What happens if maltase is denatured? *If Maltase is denatured, it can lose some of its unique properties and will most likely be unable to perform its regular functions. *Denaturing results in a permanent change to Maltase and prevents it from working appropriately.
Maltose can be broken down to glucose by the maltase enzyme, which catalyses the hydrolysis of the glycosidic bond.
Some properties of the partially purified maltase were determined: optimum pH, 6.5; optimum temperature, 48 to 50°C; pH stability range, 5.0 to 7.0; temperature stability range, 0 to 50°C; isoelectric point, pH 5.2; and molecular weight, 52,000.
maltase, enzyme that catalyzes the hydrolysis of the disaccharide maltose to the simple sugar glucose. During digestion, starch is partially transformed into maltose by the pancreatic or salivary enzymes called amylases; maltase secreted by the intestine then converts maltose into glucose.
Enzymes are proteins with specific tertiary structures. Part of this structure forms an active site. Only the substrate of an enzyme, in this case Maltose, fits/ binds to the active site.
Explain why maltase catalyses only this reaction. The enzyme maltose will always fold into in a tertiary structure, which results in the active site being in a specific shape that only the substrate maltase can bind to.
When an enzyme binds its substrate, it forms an enzyme-substrate complex. This complex lowers the activation energy of the reaction and promotes its rapid progression by providing certain ions or chemical groups that actually form covalent bonds with molecules as a necessary step of the reaction process.
The absence of acid maltase leads to an excessive accumulation of glycogen in lysosome-derived vacuoles. The presence of abnormal quantities of glycogen disrupts the normal architecture and function of the affected cells. The excess glycogen is expected to be, at least initially, in the vacuolar system.
Acid maltase deficiency in adults is associated with progressive muscle weakness and may effect respiratory muscles resulting in respiratory failure.
This is because at high temperatures (usually over 45 ºC), the protein structure of the enzyme is denatured by heat. The molecule loses its shape and the enzyme is de-activated.
Some other examples of extracellular enzymes are pepsin, chymotrypsin, elastases, collagenases, pancreatic amylase, pancreatic nucleases, and nucleosidases, etc. Moreover, intestinal enzymes such as peptidase, sucrase, and maltase are also extracellular enzymes.
Relate this ten to maltase – an enzyme (contains an active site). You can therefore say that the tertiary structure of maltase determines the shape of its active site, which is complementary in shape to a specific substrate, in this case – maltose.
In 1880, H.T. Brown discovered mucosal maltase activity and differentiated it from diastase, now called amylase. In the 1960s advances in protein chemistry allowed Arne Dahlqvist and Giorgio Semenza to fractionate and characterize small intestinal maltase activities.
Enzyme activity increases as temperature increases, and in turn increases the rate of the reaction. This also means activity decreases at colder temperatures.
The optimum temperature and pH for the trypsin are 65 °C and pH 9.0, respectively. Also, the enzyme can be significantly activated by Ba2+.
Since enzymes catalyse reactions by randomly colliding with Substrate molecules, increasing temperature increases the rate of reaction, forming more product.
High temperatures can denature enzymes, and when this happens, the active site changes and no longer binds to the substrate. 2. Explain the Lock and Key Theory of enzyme function.
Enzyme Inhibitors reduce the rate of an enzyme catalysed reaction by interfering with the enzyme in some way. Therefore less substrate molecules can bind to the enzymes so the reaction rate is decreased. Competitive Inhibition is usually temporary, and the Inhibitor eventually leaves the enzyme.
Sucrase, another activity of the dextrinase/isomaltase enzyme, cleaves sucrose to glucose and fructose.
Maltase enzyme catalyse the conversion of maltose into glucose (2 moles).
The effect of pH
Enzymes are also sensitive to pH . Changing the pH of its surroundings will also change the shape of the active site of an enzyme. Many amino acids in an enzyme molecule carry a charge . Within the enzyme molecule, positively and negatively charged amino acids will attract.
As the temperature increases so does the rate of enzyme activity. An optimum activity is reached at the enzyme’s optimum temperature. A continued increase in temperature results in a sharp decrease in activity as the enzyme’s active site changes shape. It is now denatured.