Investigating the effects of changing temperature on the activity of enzymes Background information: Renin is an enzyme that catalyses the coagulation of milk. It is found in the stomach of many animals and is used in making cheeses and junkets. It is found in the gastric juices or gastric mucosa of many mammals‚ including humans. In the human stomach‚ particularly those of infants‚ rennin works to curdle milk so that pepsin‚ another stomach enzyme‚ can further breakdown the proteins into absorbable
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solution of KMnO4 and H2SO4‚ the solution will turn colourless and it will take a specific time for the reaction to complete. By increasing the temperature‚ the time it takes (the rate) for the solution to completely change to colourless will be increased. Thus it can be said‚ that it is being hypothesized that an increase in temperature will cause an equal increase in the rate of the reaction. Method:1). Using a measuring cylinder‚ place 50 cm3 of sulphuric acid into a 250 cm3 beaker‚ add 50 cm3
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Description: A peroxidase enzyme‚ which was extracted from a brassica compestris (turnip)‚ is tested under various conditions in temperature‚ pH level‚ and competitive inhibitor (hydroxylamine). ABSTRACT: In order to determine the properties of an enzyme‚ a peroxidase enzyme was extracted from a brassica compestris (turnip) and tested under various temperatures‚ pH levels‚ and by a competitive inhibitor (hydroxylamine). The enzyme activity was measured in various ways depending on the activity
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Introduction Enzymes are catalytic proteins. The purpose of a catalyst is to speed up metabolic reactions by lowering the free energy of activation or activation energy. Activation energy is known as the amount of energy needed to push the reactants over an energy barrier‚ so that the downhill part of the reaction can begin (Campbell 151). In an enzyme catalyzed reaction‚ the enzyme binds to its substrate‚ which is the reactant an enzyme acts on. In the reactions‚ the enzymes are very specific
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and measure the enzyme activity of β-galactosidase in the different concentrations of o-Nitrophenylgalactoside (ONPG) using a spectrophotometer. The spectrophotometer was also set at 420nm‚ a wavelength which is best for recording the absorbance values for the experiment. From the results‚ 0.9mM ONPG solution has the highest absorbance and 0.1mM ONPG solution has the least. Also‚ 0.5mM ONPG solution has the highest rate of enzyme activity and it is the most efficient as the enzyme activity of the
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Enzymes are responsible for many crucial processes in living cells since they accelerate chemical reactions which would occur too slowly‚ or would lead to different products without their contribution. Enzymes are biocatalysts that usually show high affinity to a specific substrate under particular environmental conditions. The binding of the substrate and catalysis take place at a specific small region‚ around 10 amino acids‚ in the enzyme known as active site which usually represents a hydrophobic
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Investigation of the effect of metal ions on enzyme activity Objective To study the effect of two heavy metal ions‚ lead (II) ions and silver ions on the enzyme activity of invertase. Introduction Hypothesis: The rate of enzyme reaction of invertase decreases and the reaction eventually stops as the heavy metal ions inhibit the enzyme reactions. Biological principle: Heavy metal ions are non-competitive inhibitors. They do not compete with the substrates for the active sites of enzymes. They attach
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Biology Enzyme Catalase Investigation Aim: The aim of this investigation is to study and observe whether or not the concentration of hydrogen peroxide (varying from 10 – 30 millilitres) affects the rate of reaction. Hypothesis: With the increase of the concentration of Hydrogen Peroxide 3% substrate‚ I prediction that the rate of pressure increase will begin to amplify. The pressure is bound to increase because the catalase quickly reacts with the hydrogen peroxide; this is why the more substrate
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Enzymes are found in all living cells as part of their protein constitution‚ which means that they are made of chains of amino acids bound together. These molecules provide energy for the organisms by catalyzing various biochemical reactions. Most of these chemical reactions would not take place in the conditions available if the enzymes were not a present. Therefore‚ we can say that being involved as catalysts is the main and most important role of an enzyme in any organism. Furthermore‚ many reactions
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experiment were to investigate the activity of enzymes‚ components that influence the enzyme’s activity‚ identify an unknown phosphatase‚ influence of inhibitors‚ and determine if inhibition is competitive or noncompetitive. A spectrophotometer evaluated the measurement of color change over a period time due to product being formed. Determining unknown phosphatase and effects from different inhibitors were determined by varying the pH and substrate concentrations. The unknown phosphatase analyzed showed
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