anything to add "learn about this biology ia methodology "Methodology
Creating Sodium Alginate Yeast Beads (Immobilised enzymes)

Preparing the 5% sodium alginate solution
1.1. Measure out 0.5gm of sodium alginate by using a balance and spatula, and with the measuring cylinder measure out 10ml of distilled water.
1.2. Combine 0.5gm of sodium alginate with 10ml of distilled water, then mix well with a glass rod in the beaker.
1.3. Set the beaker of sodium alginate solution aside for later use.
Preparing the yeast solution
2.1. Measure out 0.5gm of dry yeast and 10ml of distilled water with a measuring cylinder.
2.2. Mix both the 0.5gm of dry yeast and 10 ml of distilled water well together with a glass rod in the beaker, until there are so more yeast visible in the mixture.
2.3. Set the beaker of yeast solution aside for later use.
Preparing the alginate yeast solution
3.1. Combine both the 5% sodium alginate solution and yeast solution together in the beaker, mix the sodium alginate and yeast solution thoroughly with glass rod.
3.2. This creates the alginate yeast solution for the making of sodium alginate beads.
3.3. Set this solution aside and prepare for next step.
Preparing the 3% calcium chloride solution
4.1. Measure out 1.4gm of calcium chloride by using a balance and spatula, and with the measuring cylinder measure out 20ml of distilled water.
4.2. Combine 1.4gm of calcium chloride with 20ml of distilled water, then mix well with a glass rod in the beaker, until no visible calcium chloride is left in the mixture.
4.3. Set the solution aside and prepare for next step.
Preparing the alginate yeast beads
5.1. Now the alginate yeast solution and the calcium chloride solution are both ready.
5.2. By using the dropper, draw up the alginate yeast solution as prepared, then hold the dropper over to the beaker which contains the calcium chloride solution.
5.3. Drop the alginate yeast solution into the beaker containing calcium chloride solution, from a high angle, to assure that the solution is fully submerged when comes in contact with the calcium chloride solution.
5.4. The beads should be observed, continue the making of alginate yeast beads until there are approximate of 60 spheres, please make sure that the beads are in similar size.
5.5. Let the beads stay in the calcium solution and hardens for 5 minutes.
5.6. Dispose the beads that stays afloat.
5.7. With the use of a strainer, strain out the spheres from the calcium chloride solution, and rinse thoroughly through distilled water.
5.8. Then put the spheres in a petri dish and store with distilled water, prepare for later use in the experiment.
Measuring the time for alginate yeast beads to rise to the surface

Prepare a 25ml measuring cylinder, label the measuring cylinder according to the concentration of hydrogen peroxide needed to be experimented with the alginate yeast beads, as 1.5%, 0.75%, 0.5%, 0.375%, 0.25% and 0%.
Fill in 20ml of 1.5% hydrogen peroxide into the corresponding the measuring cylinder that labels as 1.5%.
With the use of forceps, drop a sphere into cylinder filled with the 3% hydrogen peroxide.
Only begin the timer when all the beads has completely descends to the bottom of the measuring cylinder.
Time and record how long it take for the first bead and all the beads to rise to the surface.
Repeat the steps from #1-6, for the other concentrations (0.75%, 0.5%, 0.375%, 0.25% and 0%).

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Methodology for Creating Sodium Alginate Yeast Beads (Immobilized Enzymes)
1. Preparing the 5% Sodium Alginate Solution
Measure Sodium Alginate: Use a balance and spatula to measure out 0.5 g of sodium alginate.
Measure Distilled Water: Use a measuring cylinder to measure 10 ml of distilled water.
Mix Solution: Combine the sodium alginate with the distilled water in a beaker and mix thoroughly with a glass rod.
Set Aside: Leave the beaker of sodium alginate solution for later use.
2. Preparing the Yeast Solution
Measure Dry Yeast: Measure out 0.5 g of dry yeast.
Measure Distilled Water: Use a measuring cylinder to measure 10 ml of distilled water.
Mix Yeast and Water: Combine the yeast with the distilled water in a beaker and mix until no yeast particles are visible.
Set Aside: Leave the beaker of yeast solution for later use.
3. Preparing the Alginate Yeast Solution
Combine Solutions: Mix the 5% sodium alginate solution with the yeast solution in a beaker using a glass rod.
Set Aside: Prepare the combined alginate yeast solution for the next step.
4. Preparing the 3% Calcium Chloride Solution
Measure Calcium Chloride: Use a balance and spatula to measure 1.4 g of calcium chloride.
Measure Distilled Water: Use a measuring cylinder to measure 20 ml of distilled water.
Mix Solution: Combine the calcium chloride with the distilled water in a beaker and mix until fully dissolved.
Set Aside: Leave the calcium chloride solution for the next step.
5. Preparing the Alginate Yeast Beads
Gather Solutions: Ensure both the alginate yeast solution and calcium chloride solution are ready.
Use Dropper: Draw up the alginate yeast solution using a dropper.
Create Beads: Hold the dropper over the calcium chloride solution and release the alginate yeast solution from a height to form beads.
Repeat Process: Continue until approximately 60 beads are formed, ensuring they are similar in size.
Harden Beads: Let the beads sit in the calcium chloride solution for 5 minutes.
Remove Floats: Dispose of any beads that float.
Rinse Beads: Strain the spheres from the calcium chloride solution and rinse thoroughly with distilled water.
Store Beads: Place the beads in a petri dish with distilled water for later use.
6. Measuring the Time for Beads to Rise
Prepare Measuring Cylinder: Label a 25 ml measuring cylinder for various hydrogen peroxide concentrations: 1.5%, 0.75%, 0.5%, 0.375%, 0.25%, and 0%.
Fill with Hydrogen Peroxide: Pour 20 ml of 1.5% hydrogen peroxide into the corresponding cylinder.
Drop Bead: Use forceps to drop a bead into the cylinder filled with hydrogen peroxide.
Start Timing: Begin the timer only when the bead has completely descended to the bottom.
Record Time: Measure and record the time it takes for the first bead and all beads to rise to the surface.
Repeat for Other Concentrations: Repeat steps 1-6 for the other hydrogen peroxide concentrations.
Notes
Ensure all measurements are accurate for reproducibility.
Maintain consistent bead size for valid comparisons.
Conduct all experiments in a controlled environment to minimize variability.
now here provided are the data sets gathered "

Figure 5. Table of data for the first bead to reach the surface
Hydrogen peroxide concentration / % Initial rate of time required for (1st) yeast bead to surface / Au s-1 Mean time required for yeast bead to surface / Au s-1 Standard deviation / Au s-1
Trial 1 Trial 2 Trial 3 Trial 4 Trial 5 Trial 6
0 N/A N/A N/A N/A N/A N/A N/A N/A
0.25 127.60 104.12 146.65 141.85 151.80 151.08 137.2 16.8
0.375 66.31 74.24 88.44 96.22 101.80 93.93 86.82 12.5
0.5 59.58 69.78 62.23 67.70 77.64 57.19 65.7 6.9
0.75 52.32 40.96 40.74 40.31 44.46 49.96 44.8 4.7
1.5 37.39 27.37 23.31 23.44 22.18 24.24 26.3 5.2

Figure 6. Table of data for all beads reaching the surface
Hydrogen peroxide concentration / % Initial rate of time required for (all) yeast bead to surface / Au s-1 Mean time required for yeast bead to surface / Au s-1 Standard deviation / Au s-1
Trial 1 Trial 2 Trial 3 Trial 4 Trial 5 Trial 6
0 N/A N/A N/A N/A N/A N/A N/A N/A
0.25 137.52 123.62 169.43 164.71 169.73 165.01 155.0 17.8
0.375 84.27 87.04 107.92 105.22 117.77 110.98 102.2 12.3
0.5 68.36 76.14 80.37 78.09 79.72 74.61 63.2 28.5
0.75 61.92 48.01 48.62 50.54 53.72 55.04 53.0 4.7
1.5 45.79 29.49 25.31 27.66 26.13 29.21 30.6 6.9
*Note:
• Mean and standard deviation are rounded to 1 decimal place (1 d.p.), for maintaining the precision of time measured
• Timer stops at 4 minutes for 0% after no reaction available for recording

"

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Data Analysis of Yeast Bead Surface Rise
Figure 5: Time for the First Yeast Bead to Surface
Hydrogen Peroxide Concentration (%)	Trial 1	Trial 2	Trial 3	Trial 4	Trial 5	Trial 6	Mean (Au s⁻¹)	Standard Deviation (Au s⁻¹)
0	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A
0.25	127.60	104.12	146.65	141.85	151.80	151.08	137.2	16.8
0.375	66.31	74.24	88.44	96.22	101.80	93.93	86.82	12.5
0.5	59.58	69.78	62.23	67.70	77.64	57.19	65.7	6.9
0.75	52.32	40.96	40.74	40.31	44.46	49.96	44.8	4.7
1.5	37.39	27.37	23.31	23.44	22.18	24.24	26.3	5.2
Figure 6: Time for All Yeast Beads to Surface
Hydrogen Peroxide Concentration (%)	Trial 1	Trial 2	Trial 3	Trial 4	Trial 5	Trial 6	Mean (Au s⁻¹)	Standard Deviation (Au s⁻¹)
0	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A
0.25	137.52	123.62	169.43	164.71	169.73	165.01	155.0	17.8
0.375	84.27	87.04	107.92	105.22	117.77	110.98	102.2	12.3
0.5	68.36	76.14	80.37	78.09	79.72	74.61	63.2	28.5
0.75	61.92	48.01	48.62	50.54	53.72	55.04	53.0	4.7
1.5	45.79	29.49	25.31	27.66	26.13	29.21	30.6	6.9
Notes
Mean Values: Calculated for each concentration based on the trials.
Standard Deviation: Indicates variability in the time measurements for each concentration.
N/A Values: Represent cases where no reaction was recorded (e.g., 0% concentration).
Observation: As the concentration of hydrogen peroxide increases, the mean time for beads to rise decreases, indicating a more rapid reaction.
Conclusion
The data suggests that higher concentrations of hydrogen peroxide lead to a faster ascent of the yeast beads, indicating enhanced enzymatic activity or reaction kinetics in the presence of the substrate. Further analysis may explore the relationship between concentration and the rate of reaction in greater detail.

here is also the statistical analysis "Statistical Analysis
As there are five categories of results from five different concentrations analysed, independent groups of hydrogen peroxide concentration are being investigated, performed by a Kruskal-Wallis One Way ANOVA test by Ranks. Using this method, the F statistic value found was 59.1645, corresponding to a <0.0001 P-value, also larger than the H-critical value of 3.07. Hence by conventional criteria, it is lower than the standard significance level of 0.05. This value is then considered to be extremely statistically significant and not by chance. Suggesting that the concentration of hydrogen peroxide does influence the rate of reaction.
Therefore, despite potential overlapping error bars, the data is proven to be relatively reliable and the null hypothesis is rejected.
"

for the data analysis please formulate and answer all the following questions
"- Interpret the patterns and trends in the data, refer to tables and graphs when reporting numbers/trends [A4.1]. How do these relate to RQ? [A4.4]
⁃
⁃
Discuss the variation (SD) in the data and possible anomalies [A4.2] + [A4.3]
Discuss the uncertainty of your data (p value, critical value for stats tests - do you accept or reject null/alternative hypothesis?). Was enough data collected to make a valid conclusion? [A3.3] Do you need to remove data, and if so, does this impact your findings? [A3.1]
Conclusion
⁃ Do the trends/patterns have problems making it difficult to be certain (St.Dev., p value, t-test)? [EV3.1]
What scientific explanation are there for your observed results? [EV2.1] Provide scientific references for this [EV2.2] How do your results compare to those of previously conducted investigations/research data? [EV2.3] What does this mean for your context? [EV2.4] Provide a conclusion based on your data and analysis. Was your hypothesis correct? Does it answer your RQ? [EV1.2] Is this conclusion strong - why or why not? [EV1.3]
"

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Data Analysis and Interpretation
Patterns and Trends in the Data [A4.1]
The data reveals a clear trend: as the concentration of hydrogen peroxide increases, the time taken for the yeast beads to surface decreases.

Table 5 indicates that at 0.25% concentration, the average time for the first bead to surface is 137.2 Au s⁻¹, while at 1.5%, it drops significantly to 26.3 Au s⁻¹. This trend is mirrored in Table 6, where the average time for all beads to surface also decreases from 155.0 Au s⁻¹ at 0.25% to 30.6 Au s⁻¹ at 1.5%.
This observation supports the research question (RQ) regarding the effect of hydrogen peroxide concentration on the reaction rate, indicating a direct relationship between concentration and enzymatic activity.

Variation and Possible Anomalies [A4.2] + [A4.3]
The standard deviation (SD) values across trials show varying degrees of consistency:

0.25% has an SD of 16.8, while 1.5% has a lower SD of 5.2, indicating more reliable measurements at higher concentrations.
The 0.5% concentration has a notably high SD of 28.5, suggesting some anomalies or variability in the data. This could be due to experimental errors or differences in bead size affecting buoyancy.
Uncertainty of Data and Hypothesis Testing [A3.3]
The Kruskal-Wallis test yielded an F statistic of 59.1645 with a p-value < 0.0001, indicating a highly significant difference between groups. Given that the p-value is much lower than the standard significance level of 0.05, we reject the null hypothesis. This result suggests that hydrogen peroxide concentration significantly influences the reaction rate.

The dataset appears sufficient to draw valid conclusions, but if any data points were removed, particularly those with high variability, it might impact the overall findings. However, the strong statistical significance indicates the robustness of the results.

Conclusion
While the trends are clear, the variability (SD) and presence of anomalies could create some uncertainty in specific conclusions. The highly significant p-value supports the reliability of the findings, but the variations in SD highlight the need for cautious interpretation.

Scientific Explanation for Observed Results [EV2.1]
The observed results can be explained by the principle that higher concentrations of hydrogen peroxide provide more substrate for the yeast enzymes to act upon, enhancing the rate of enzymatic reactions. The enzyme catalase, found in yeast, breaks down hydrogen peroxide into water and oxygen, leading to increased gas production and faster ascent of the beads.

Comparison to Previous Research [EV2.3]
Previous studies have shown similar trends where increased substrate concentrations lead to heightened reaction rates in enzyme-catalyzed processes. For instance, research on catalase activity has consistently demonstrated that reaction rates increase with substrate concentration until a saturation point is reached.

Implications for Context [EV2.4]
These findings suggest that in applications utilizing yeast and hydrogen peroxide, such as in bioengineering or food processing, optimizing hydrogen peroxide concentrations can enhance reaction efficiency. This has practical implications for industrial processes that rely on enzymatic reactions.

Conclusion Based on Data and Analysis [EV1.2]
The hypothesis that higher hydrogen peroxide concentrations lead to faster yeast bead ascent is supported by the data. The results confirm the research question, demonstrating a clear relationship between concentration and reaction rate.

Strength of Conclusion [EV1.3]
The conclusion is strong due to the significant statistical results and clear trends observed in the data. Despite some variability, the overall analysis indicates a reliable relationship that can be applied in practical contexts. Further studies could enhance understanding and address any remaining uncertainties.

learn the writing structure in this conclusion "The experiment demonstrates that as the ethanol concentration in the medium increases, the rate of digestion reduces, as evidenced by a higher intensity of the ultimate blue-black hue resulting from the starch-triiodide complex formed between iodine and unhydrolyzed starch. This is consistent with the hypothesis and
premise that higher ethanol concentrations result in reduced enzyme activity.
The residual catalytic activity could be observed despite a 100% ethanol concentration. Therefore, it can be concluded that using 100% ethanol will not cause the total loss of functionality of the active site of amylase, which is not overly surprising, given that ethanol, much like water, is predominantly a polar
solvent.
As brought up in the analysis section, the ANOVA test shows that ethanol treatment at each concentration produces a statistically significant decrease in the rate of starch hydrolysis. There are many possible molecular mechanisms by which ethanol reduces enzyme activity. Enzymes are proteins, and their function depends on their ability to maintain an appropriate three-dimensional shape. One possible cause for the decrease in the rate of reaction is the induced unfolding of proteins (Moeller). Most enzymes are naturally globular proteins with lots of hydrophilic amino acid residues on their exteriors to enhance their aqueous solubility. Replacing the natural external aqueous environment with increasing concentrations of lower- polarity solvents, such as ethanol, could “remove the layer of hydration surrounding the enzyme” (Wang et al.), leading to structural instability. One piece of further investigation revealed that the addition of alcohols, a polar molecule with a short hydrocarbon section, can reduce nonlocal hydrophobic interactions while increasing local polar interactions (Singh et al.). This results in the destabilization of the protein's native hydrophobic core and an increase in the formation of local hydrogen bonds, leading to the formation
of extended secondary structures, i.e., denaturation.
Another more specific piece of research (Vernon-Carter et al.) studied how pancreatic amylase activity towards corn starch is affected by ethanol, with the study offering mechanistic insight. The authors claim with Infrared (IR) spectroscopy evidence that was using ethanol as a co-solvent with water, up to 5%, promotes the formation of beta-pleated sheets, which are compact secondary structures of the active site
that “impose conformational problems for the binding of with starch chains.”
Furthermore, a specific study on ethanol in beer on α-amylase activity reveals that “Through computational analysis, it was shown that the conformation of α-amylase changed from globular to elongated structures, suggested to arise from the uncoiling of the polypeptide chain as a result of ethanol denaturation. This common type of alcohol denaturation disrupts the globular protein structure's hydrogen bonds while forming new hydrogen bonds between its polypeptide chain (Ramsey et al.). As a result, there is a
decreasing number of hydrophilic pockets”.
In addition, the hypothesis for the observed decrease in starch hydrolysis involves ethanol acting as an inhibitor. Research has shown that ethanol can serve as a reversible non-competitive inhibitor (Malfait et al.). While no mechanistic insight was offered within the paper, the authors provided graphical evidence that the Vmax of the reaction decreased, whereas the Michaelis-Menten constant remained unchanged. The fact that the mode of inhibition is non-competitive rather than competitive is consistent with the fact that ethanol has a very different chemical structure from starch and binds to the allosteric site rather than the active site. The authors further reported that there was little sign of amylase denaturation, which can be isolated and reused. However, the concentration employed during their report peaked at about 9%,
significantly lower than the experimental results obtained from my investigation." and formulate a new one based off my data and questions

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Conclusion
The experiment demonstrates that as hydrogen peroxide concentration increases, the time taken for yeast beads to surface decreases, as evidenced by the mean ascent times recorded in Tables 5 and 6. This trend supports the hypothesis that higher concentrations of hydrogen peroxide enhance enzymatic activity, specifically the activity of catalase in yeast, leading to more rapid gas production.

Interestingly, even at the highest concentration of 1.5%, some catalytic activity persisted, suggesting that total enzyme inactivity is not achieved even under extreme conditions. This aligns with the understanding that while hydrogen peroxide can inhibit enzyme function, it does not completely denature catalase, which is consistent with its role as a polar solvent.

The Kruskal-Wallis statistical analysis confirms that the differences in reaction rates across concentrations are statistically significant, with an F statistic of 59.1645 and a p-value of less than 0.0001. This indicates that the concentration of hydrogen peroxide indeed influences the rate of yeast bead ascent, rejecting the null hypothesis.

Several molecular mechanisms may explain the observed results. Higher concentrations of hydrogen peroxide increase substrate availability for the catalase enzyme, facilitating more rapid breakdown of hydrogen peroxide into water and oxygen. Additionally, it is important to note that while higher concentrations enhance activity, they may also induce structural changes in the enzyme, potentially affecting its efficiency.

Research indicates that enzyme activity can be influenced by changes in the enzyme's three-dimensional structure. As hydrogen peroxide concentration rises, it could lead to denaturation or alterations in enzyme conformation, which may create a balance between increased activity due to substrate concentration and decreased activity due to structural instability.

Furthermore, previous studies have shown similar trends where increased substrate concentration leads to heightened enzymatic activity until a saturation point is reached. This is consistent with the findings in this investigation, where varying hydrogen peroxide concentrations resulted in significant differences in reaction rates.

In conclusion, the data strongly supports the hypothesis that higher hydrogen peroxide concentrations correlate with increased rates of reaction in yeast, answering the research question effectively. The conclusion is robust due to the significant statistical evidence and clear trends observed. However, the presence of variability in the data suggests that further investigations could provide additional insights into the mechanistic details of enzyme activity under varying conditions."