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Salivary Amylase And Phosphorylase As B

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Salivary Amylase And Phosphorylase As B
Introduction: The purpose of this lab was to check the time needed for salivary amylase and phosphorylase to produce a negative result and how different concentrations affected those times. Enzymes are biological catalysts that can cause a specific chemical change in any part of the body (Walsh, 2002). Many of the reactions that take place within a cell would normally take place at temperatures substantially higher than those present inside a cell (Alberts et al., 2010). Because of this, these chemical reactions require the assistance of enzymes to catalyze the reaction and allow it reaction to occur quickly (Alberts et al., 2010). The substrate binds with the active site on the enzyme to form a substrate enzyme complex (Di Giuseppe, 2002). The substrate is then transformed into one or more products, which are released from the active site and the enzyme remains unaltered (Di Giuseppe, 2002). Salivary amylase is a digestive enzyme found in saliva that acts on starch to begin the digestion process (Stick and Williams, 2009). Amylase acts on starch by breaking off maltose (C12H22O11) molecules from the end of starch chains (Di Giuseppe, 2002). Every time a bond is broken in a starch chain, a water molecule is consumed. This process is referred to as a hydrolysis reaction which requires water to digest a substrate, in this case starch (Walsh, 2002). Phosphorylase is also an enzyme that acts on starch by removing glucose molecules (Stick and Williams, 2009). Phosphorylase breaks down the bonds between adjacent molecules in starch by consuming phosphoric acid instead of water like amylase (Stick and Williams, 2010). The energy released in this exergonic reaction is used to create a glucose phosphate bond in glucose-1-phosphate. Water is a medium in this reaction, not a product or reaction. The concentration of water will not affect the direction of the reaction because it is not directly in use. A starch primer molecule is necessary for a positive

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