pepsin
The digestion of milk fats by pancreatic lipase and the digestion of proteins by pepsin and trypsin
By Jenny Lam
Abstract
The purpose of this project was to determine how pancreatic lipase and bile salts digest fats to fatty acids and glycerol and how pepsin and tryspin digest to polypeptides. Litmus solution (pH indicator) was used for the fats to indicate the occurrence of the digestion of fats in experiment A. Egg whites was used as the substrate for the enzymes in experiment B. The pH was adjusted to drops of hydrochloric acid and sodium hydroxide. The temperature was established in the water bath at 37°C and then in the incubator. The change in egg white appearance was determined by placing it out of the water bath and into the incubator for an hour. The results showed that pepsin at a pH of 2 did better at lower temperatures while the trypsin at a pH of 8 did better at higher temperatures. The hypothesis was not stated for this study.
The digestion of milk fats by pancreatic lipase and the digestion of pepsin and trypsin
Enzymes are the biological protein molecules that act as catalyst inside the cell. This means, they either assist or increase the rate of reactions that occur without undergoing any chemical change during the reaction, as well as catalysing all the metabolic reactions of cells. They are made up of amino acids linked together to form multiple polypeptide chains and their function is determined by their complex structure (Brian, Marshall 2013, How Cells Work).
Enzymes contain specific binding sites, called active sites, where chemical reactions are catalysed and the rest of the protein acts as scaffolding, supporting the active site and allowing it to maintain its proper shape. In a chemical reaction, the reactants, or substrates, binds to the active site of the enzyme, where amino acids are attached to the substrate molecule and held in position while the reaction takes place. This forms
By Jenny Lam
Abstract
The purpose of this project was to determine how pancreatic lipase and bile salts digest fats to fatty acids and glycerol and how pepsin and tryspin digest to polypeptides. Litmus solution (pH indicator) was used for the fats to indicate the occurrence of the digestion of fats in experiment A. Egg whites was used as the substrate for the enzymes in experiment B. The pH was adjusted to drops of hydrochloric acid and sodium hydroxide. The temperature was established in the water bath at 37°C and then in the incubator. The change in egg white appearance was determined by placing it out of the water bath and into the incubator for an hour. The results showed that pepsin at a pH of 2 did better at lower temperatures while the trypsin at a pH of 8 did better at higher temperatures. The hypothesis was not stated for this study.
The digestion of milk fats by pancreatic lipase and the digestion of pepsin and trypsin
Enzymes are the biological protein molecules that act as catalyst inside the cell. This means, they either assist or increase the rate of reactions that occur without undergoing any chemical change during the reaction, as well as catalysing all the metabolic reactions of cells. They are made up of amino acids linked together to form multiple polypeptide chains and their function is determined by their complex structure (Brian, Marshall 2013, How Cells Work).
Enzymes contain specific binding sites, called active sites, where chemical reactions are catalysed and the rest of the protein acts as scaffolding, supporting the active site and allowing it to maintain its proper shape. In a chemical reaction, the reactants, or substrates, binds to the active site of the enzyme, where amino acids are attached to the substrate molecule and held in position while the reaction takes place. This forms
Bibliography: Controlling Enzymes 2012, viewed 19 May 2013, Introduction to Enzymes 2011, viewed 18 May 2013, Lipase 2011, viewed 20 May 2013, Marshall, Brian 2013, How Cells Work, viewed 19 May 2013, Thibodeaux, Wanda 2013, What Is the Function of Pepsin in Digestion?, viewed 21 May 2013, Wolfe, Marni 2011, What Are the Functions of Trypsin?, viewed 21 May 2013,