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The test for amylase is easier to perform than that for lipase, making it the primary test used to detect and monitor pancreatitis. Medical laboratories will usually measure either pancreatic amylase or total amylase. If only pancreatic amylase is measured, an increase will not be noted with mumps or other salivary gland trauma.
Effects of different types of inhibition on the double-reciprocal plot. When used for determining the type of enzyme inhibition, the Lineweaver–Burk plot can distinguish between competitive, pure non-competitive and uncompetitive inhibitors. The various modes of inhibition can be compared to the uninhibited reaction.
The γ-amylase has the most acidic optimum pH of all amylases because it is most active around pH 3. They belong to a variety of different glycoside hydrolase families, such as glycoside hydrolase family 15 in fungi, glycoside hydrolase family 31 of human MGAM , and glycoside hydrolase family 97 of bacterial forms.
The rate of a reaction is the concentration of substrate disappearing (or product produced) per unit time (mol L −1 s −1). The % purity is 100% × (specific activity of enzyme sample / specific activity of pure enzyme). The impure sample has lower specific activity because some of the mass is not actually enzyme.
β-Amylase (EC 3.2.1.2, saccharogen amylase, glycogenase) is an enzyme with the systematic name 4-α-D-glucan maltohydrolase. [ 2 ] [ 3 ] [ 4 ] It catalyses the following reaction: Hydrolysis of (1→4)-α- D -glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
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The effects of temperature on enzyme activity. Top: increasing temperature increases the rate of reaction (Q10 coefficient). Middle: the fraction of folded and functional enzyme decreases above its denaturation temperature. Bottom: consequently, an enzyme's optimal rate of reaction is at an intermediate temperature.