Effect Of Substrate Concentration On The Activity Of The Enzyme Catalase A Level Biology Project Aims This is an experiment to examine how the concentration of the substrate hydrogen peroxide affects the rate of reaction of the enzyme catalase. Background Information Enzymes such as Catalase are protein molecules which are found in living cells. They are used to speed up specific reactions in the cells. They are all very specific as each enzyme just performs one particular reaction. Catalase is
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inside of the amylose coil.The amount of blue complex that starch gives with iodine can be measured by using a spectrophotometer. α-amylases are found in saliva‚ pancreatic juice‚ human breast milk‚ serum and certain tissues such as the liver. This enzyme catalyzes the hydrolysis of α (1-4) linkages in starch by breaking it down to maltose and some glucose. As the starch is broken down‚ the coiled structure of α-amylase is unfolded. Therefore‚ iodine will no longer be able to form the blue complex
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to observe how molarity concentration affects diffusion.The lab was primarily based on osmosis and diffusion. Diffusion is when the movement of molecules from a high concentration that go to a low concentration to a high concentration to eventually reach an equilibrium. Osmosis is when water will diffuse from high water concentration to low water concentration to reach equilibrium. When the solutions are different the lower concentration solute is hypotonic while the higher concentration solute is
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Finding the Optimal pH of the Enzyme Peroxidase with the Aid of a Spectrophotometer ABSTRACT The peroxidase enzyme was partially purified‚ and the enzyme activity was calculated with the use of a spectrophotometer‚ demonstrating the effect of pH on peroxidase activity. The objective of this exercise was to determine the ideal pH for peroxidase activity. The data concluded that the optimum pH for peroxidase activity is 5‚ and the “standardized” enzyme volume is 2.8mL.
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RESULTS AND DISCUSSION REPORT—EXPERIMENT 3 (CHEMICAL KINETICS) CALCULATIONS Effect of Concentration on Reaction Rate [S2O32-]initand [H+]init for each run‚ knowing the original concentrations and volumes of [S2O32-]‚ [H+]‚ and water used. [S2O32-]init= __(M[S2O32-])(V[S2O32-])__ [H+]init= _____(M[H+])(V[H+])____ V[S2O32-]+V[H+]+V[water] V[H+]+V[S2O32-]+V[water] Run 1 [S2O32-]init= (0.15 M)(10 mL) (10+3+2)mL = 0.1 M [H+]init= (3 M)(2
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manuscript. (Page 8‚ line 13-15) Comment 14: Page 8: Explain if pH was controlled during fermentation. In any case‚ do a reference in the result section to the pH at the end of fermentation Response: The pH was not directly controlled during the fermentation. In the line with typical studies conducted for ABE production‚ the medium was supplemented with buffer (50 g/L KH2PO4‚ 50 g/L K2HPO4‚ 220 g/L C2H3O2NH4) as an approach to control the pH changes during the fermentation. In addition‚ it has been reported
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Determination of the activation energy of an enzyme catalysed reaction Introduction In this practical the aim for this experiment was to find out the catalytic power of alkaline phosphate‚ as well as the rate of reaction and the activation energy of p-nitrophenol phosphate. Enzymes are biological molecules that catalyse a chemical reaction. ‘Enzymes work by lowering the activation energy of a chemical reaction making it easier to proceed’ [1]. This allows molecules to have more energy therefore
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Bean Growth with Different pH Levels Through this experiment‚ the objective was to find which pH liquid created the best environment for the Mung beans to grow. First‚ the beans were placed into bags with different pH liquids. Then‚ measurements were taken each day to monitor the growth average of the beans. The pH 2 beans average size at the end of the experiment were 0.24 cubic centimeters‚ the pH 7 size average was 0.38 cubic centimeters‚ and the size average of the pH 2 beans was 0.24 cubic centimeters
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Research Question: To investigate how varying the pH of bromothymol blue affects the absorbance value of the solution which determines the equilibrium constant (pKa) of the indicator. Variables: Variables Variables Measured Method of measurement Independent pH of the six buffer solution A pH probe attached to a data-logger will be used to measure pH Dependent Absorption of the buffer solutions at wavelength 435.0nm and 617.0 nm A spectrophotometer (±0.001) will be used to measure absorbance
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Effect of an Increasing Substrate Concentration on Enzyme Activity Rate Abstract The reaction rate of an enzyme can be affected by many factors‚ and the purpose of this experiment was to find out how an increasing substrate concentration influences the rate of an enzyme activity; we obtained data from recording the absorbance of the samples which contain the same amount of potato juice (enzyme oxidase) and different amount of catechol (substrate) while holding pH and temperature constant. Our findings
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