Effect Of Increasing Concentration Of Yeast Invertase On Sucrose

Enzymes react differently under different conditions and concentrations, being the most productive at the enzymes specific optimum condition and concentration. The enzyme sucrase, extracted from yeast, breaks down the complex sugar sucrose into the simple sugar glucose. Testing for sucrase’s optimum environment, multiple reactions were ran using varying amounts and concentrations of sucrose and sucrase at different pHs and temperatures. The product was then treated with Benedicts solution to visually observe what amount of glucose was present after the reaction was ran; negative results being little to no glucose present and positive results being

Observe: Wait until the numbers are not changing very much. What do you notice about the solute concentrations inside and outside of the cell? _______________________________

Yeast is a fungus that can generate glucose into energy without using any oxygen molecules. We tested the fermenting ability of yeast from two different carbon sources: glucose and aspartame. We hypothesized that yeast is unable to use the carbon sources of aspartame. To do this, we decided to use both carbon sources in the same concentration. Each carbon source was mixed with the same amount of yeast solution. The experiment group of 5.5 mM aspartame solution was compared with the control group of 5.5mM glucose solution. We recorded the rate of fermentation for glucose and aspartame in the Vernier Lab Quest. The fermentation rate of aspartame is a negative number, and glucose is a positive number. Our results show that yeast was unable to ferment aspartame as yeast fermented glucose. The results indicate that aspartame has no effect on yeast fermentation rate because yeast do not catabolize aspartame because it does not have the appropriate enzymes to break it down.

During this experiment, sugar sources were varied and respiration rate evaluated. To begin, a water bath was set at 30 degrees Celsius. This creates an optimum temperature for the enzymes in yeast to breakdown sugar and give off CO₂. Each sugar source, glucose, sucrose, lactose and glycerol were all added to its own unique yeast sample, one at a time. Each sugar source that was added to the yeast solution was immediately incubated for 10 min, then was transferred to a respiration chamber. The CO₂ sensor was put in, recording the CO₂ respiration for 4 min. This process was done for each sugar source. The reparation rate was recorded through Logger Pro. After 4 min passed, the slope was recorded, resulting in respiration rate.

Our purpose in this lab was to create four solutions of the same components and different concentration. I found the concentration in Molarity (mol/liter). I would dilute a solution to create new solutions, using the formula M1xV1=M2xV2 where M=molarity and V=volume. In this lab, there were four solutions, Solution A, Solution B, Solution C, and Solution D. The solute or substance that dissolves was sugar and the solvent or substance that the solute dissolves in was water. For Solution A, I weighed 3.42 g sugar and diluted to 100 mL to get a concentration of 0.10 M and the color of bright red. For Solution B, I weighed 0.342 g sugar and diluted to 100 mL to get a concentration of 0.010 M and the color of pink. For Solution C, I measured 10

Is this a linear relationship? What happens to the initial reaction rate as substrate concentration increases?

The purpose of this experiment was to record catalase enzyme activity with different temperatures and substrate concentrations. It was hypothesized that, until all active sites were bound, as the substrate concentration increased, the reaction rate would increase. The first experiment consisted of five different substrate concentrations, 0.8%, 0.4%, 0.2%, 0.1%, and 0% H2O2. The second experiment was completed using 0.8% substrate concentration and four different temperatures of enzymes ranging from cold to boiled. It was hypothesized that as the temperature increased, the reaction rate would increase. This would occur until the enzyme was denatured. The results from the two experiments show that the more substrate concentration,

1.2 1.0 0.8 0.6 0.4 0.2 0.0 0.0 1.0 2.0 3.0 4.0 5.0 6.0 7.0 Concentration (mM) y = 0.1897x R2 = 0.99

This lab investigates the effects of Sucrose concentration on cell respiration in yeast. Yeast produces ethyl alcohol and CO2 as a byproduct of anaerobic cellular respiration, so we measured the rate of cellular respiration by the amount of CO2

This experiment is to study 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 ONPG solution continues even though the other concentrations of ONPG solution has already stopped the enzymatic reactions as the substrate is already used up.

Enzymes are high molecular weight molecules and are proteins in nature. Enzymes work as catalysts in biochemical reactions in living organisms. Enzyme Catecholase is found on in plants, animals as well as fungi and is responsible for the darkening of different fruits. In most cases enzymatic activities are influenced by a number of factors, among them is temperature, PH, enzyme concentration as well as substrate concentration (Silverthorn, 2004). In this experiment enzyme catecholase was used to investigate the effects of PH and enzyme concentration on it rate of reaction. A pH buffer was used to control the PH, potato juice was used as the substrate and water was used as a solvent.

In the exercise # 2 we observed the effect of substrate concentration, enzyme concentration, pH and temperature on enzyme activity. All the data showed that once potato extract was added to catechol and water the reaction varied dependent on the level of catechol. As in

The effect was tested of a varying substrate concentration on the rate of an enzyme-catalase reaction. We also tested the effect of temperature on the rate of an enzyme-catalase reaction. Our hypothesis for the variation of substrate was that if the substrate increases, then the reaction rate will be quicker.

According to the graph, it shows that the enzyme-catalyzed reaction performs the best as the temperature increases to 30’C. The rate declines as the temperature increases over 30 and it no longer works at 70. When the surrounding temperature increases to 30, the reactant absorbs enough energy to top of the activation energy barrier and the reaction occurs. As the temperature inclines, there begins an increase in molecular movement which leads to an increasing rate of reaction, in this case, producing more bubbles of gas. However, as the temperature get high, the transition state of molecules is reached rarely that the reaction will hardly proceed at all. Therefore, in the environment where the temperature higher than 30C, the molecular movement

2. Following solutions are added to the tubes and the pH of each tube is determined: