The Effect of pH, Temperature, and Enzyme concentration on Enzymatic Activity3

Pareja, Ma. Micaela V.

Peñaranda, Marcus Arveinzl O.

Uy, Frederick

Visperas, Justine May G.

Group 2 - BS BIOLOGY lllA (SET B)

October 22, 2024

A scientific paper submitted in partial fulfillment of the requirements in General Physiology Laboratory
under Ms. Darlene Faye Cadao, 1st Semester 2024-2025.
 ABSTRACT
An enzyme is a biological catalyst, mostly a protein. Enzymes interact with substrate molecules
and reduce the activation energy required for chemical processes by stabilizing the transition state.
Enzymes are affected by several factors, including temperature and pH. Without enzymes, most
metabolic reactions would take longer and not be fast enough to sustain enzymatic activity. Different
experimentations were performed to explore the factors influencing enzymatic activity, including
catalase, bromelain, and amylase, analyzing their result on hydrogen peroxide, proteins, and
starch. Each result was observed and analyzed under different conditions, and the reaction rate
would increase or decrease depending on the enzyme and substrate concentration. Hence, this
experiment emphasizes the role of enzymes in how factors, including temperature and pH, affect
the reaction rate.
Keywords: enzymes, temperature, pH, catalase, bromelain, amylase, hydrogen peroxide, proteins,
starch

1
 INTRODUCTION

In our daily lives, numerous chemical reactions occur in our body to facilitate essential metabolic
processes (Lewis & Stone, 2023). An enzyme is a biological catalyst, mostly a protein (Austin, 2022).
Enzymes indicate two vital properties. First, they increase chemical processes without being consumed or
altered by the reaction. Second, they increase chemical processes without changing the chemical
equilibrium between reactants and products (Cooper, 2000)

Enzymes interact with substrate molecules and reduce the activation energy required for chemical
processes by stabilizing the transition state. This stabilization increased the reaction rates, enabling them
to occur at physiologically significant rates. Enzymes bind with substrates at specific regions in their
structure called active sites. They are often highly specific and bind just certain substrates for particular
reactions. Without enzymes, most metabolic reactions would take longer and not be fast enough to sustain
life (Lewis & Stone, 2023). There are six (6) main types of enzymes: oxidoreductases, hydrolases,
transferases, lyases, isomerases, and ligases. Each category exhibits a general type of reaction, although
it catalyzes different specific reactions with its category (Lewis & Stone, 2023).

Some enzymes require non-protein cofactors or coenzymes for their reaction. A cofactor is an
additional chemical component that directly participates in the catalytic process and is necessary for
enzymatic activity. It can be an organic molecule, such as a vitamin or inorganic metal ion, while some
enzymes require both. A cofactor might be either tightly or loosely bound to the enzyme. If tightly associated,
the cofactor is termed a prosthetic group (Rogers, 2019). An enzyme that requires a cofactor for its activity
is called an apoenzyme (inactive enzyme), and an apoenzyme with a cofactor is referred to as a
holoenzyme (active enzyme) (Robinson, 2015).

In most chemical reactions, temperature and pH affect the rate of enzymatic activity. The increase
in temperature increases the rate of reaction. If the reactants are heated, the molecules travel more quickly
and are more likely to collide with sufficient energy to overcome the activation energy of the reactants
(Moran, 2019). Enzymes are affected by changes in pH. Extreme pH levels often lead to total loss of
enzymatic activity, since pH is a factor in the stability of enzymes (Worthington Biochemical Corporation,
2023). Each enzyme has an optimal pH at which it functions at its optimum rate. A change in pH will induce
the conformational shape in the active site. The substrate cannot bind to the active site, making the enzyme
incapable of catalyzing reaction anymore. In several cases, enzyme activity is restored when the pH
recovers to its optimal range (Moran, 2019).

The researchers hypothesized that factors such as temperature, pH, and enzyme concentration
have a significant effect on the enzyme activity. This is reasoned from the principle that enzymes have
optimum conditions in order to function properly, altering these conditions such as raising the temperature,
lowering pH, or increasing enzyme concentration may affect the activity of the enzyme. The objective of the
study aimed to study enzymatic activity and determine the effects of factors such as temperature, pH, and
enzymatic reaction on enzymatic reactions in four (4) different experiments.

MATERIALS AND METHOD

This series of experiments explores the factors that influence enzyme activity. We will examine
catalase, bromelain, and amylase, studying their effects on hydrogen peroxide, proteins, and starch,
respectively. By measuring reaction rates and observing changes in enzyme behavior under different
conditions, we aim to understand the principles governing enzyme function and their importance in
biological processes.

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 A. Catalase

Materials:

2 Test tubes 1 tripod

6 Fresh Potato tuber strips (2 cm x 0.5 1 wire gauze

cm)
1 test tube rack
Hydrogen Peroxide
Forceps
20 ml water
Wooden block
1 beaker (250 ml)
Ruler
1 Graduated cylinder (10ml)
Knife
1 Graduated cylinder (50ml)
Marker
1 Alcohol lamp

A1. Experiment Preparation

To investigate the activity of catalase in potato tubers, two test tubes were labeled 1 and 2,
each containing 5 ml of hydrogen peroxide. Six potato strips, measuring 2 cm by 0.5 cm,
were prepared from freshly peeled potato tubers using a sharp knife. Three of these strips
were boiled in 20 ml of water for five minutes to denature the enzymes, while the other
three remained unboiled.

The unboiled potato strips were then placed into test tube 1, and the boiled strips were
placed into test tube 2. Both tubes were observed for any gas evolution, which would
indicate the presence of active catalase. The boiled potato strips served as a control group
to compare the activity of catalase in unboiled potato tubers.

Figure 3.1 shows the laboratory materials Figure 3.2. Cutting 6 pcs of potatoes measured
required for the catalase experiment, including 2 cm x 0.5 cm each
two test tubes, a test tube rack, an alcohol lamp,
wire gauze, a 250 mL beaker, wooden block, a
tripod, a 50 mL graduated cylinder, and forceps. 3
Figure 3.3. Boiling the 3 pcs of potato tubers for 5
Figure 3.4. Test tube 1 contains fresh potato
minutes
tubers while test tube 2 contains boiled
potato tubers. Both tubes contain
hydrogen peroxide

B. The Bromelain Enzyme and Effect of heating on Bromelain.

Materials: Cold water

2 Apple (1 inch x 1 inch) 1 beaker (250 ml)

2 Orange (1 inch x 1 inch) Gelatin

2 Pineapple (1 inch x 1 inch) 2 small plastic containers

Knife Aluminum foil

Ruler Marker

Microwave oven

B1. Experiment Preparation

To investigate the effect of heating on bromelain, three fruits (apple, orange, and pineapple)
were each cut into two equal-sized pieces measuring 1 inch by 1 inch using a sharp knife.
One piece from each fruit was microwaved for 1-2 minutes to simulate heating, while the
other pieces remained unheated. All pieces were then cooled to room temperature by
submerging them briefly in cold water.

A gelatin solution was prepared by heating 1 teaspoon of gelatin in 100 ml of distilled water
until dissolved. The cooled gelatin solution was then divided into two small plastic
containers. Pieces of each fruit, both heated and unheated, were placed on top of the
gelatin in the respective containers. The containers were then left undisturbed for at least
1 hour, allowing the bromelain enzyme in the fruits to interact with the gelatin.

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 After an hour, the fruit pieces were removed, and the surface of the gelatin underneath was
observed and recorded. The degree of gelatinization, which indicates the activity of the
bromelain enzyme, was compared between the heated and unheated fruit samples.

Figure 3.5 Cooked gelatin topped with fresh fruits Figure 3.6 Cooked gelatin with topped
such as apple orange and pineapple microwaved fruits (apple orange
measured as 1 inch by 1 inch each. pineapple)

Figure 3.7 Cooked gelatin topped with fresh fruits

covered by aluminum foil such as apple
orange and pineapple measured as 1
inch by 1 inch each.

C. Effect of pH on Enzyme Activity (Starch and Amylase).

Materials:
5 Plastic cups Sugar
50 ml Water Starch
1 Graduated cylinder (10ml) Betadine
Saliva 3 Dropper
Vinegar Marker

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 C1. Experiment Preparation

To investigate the effect of pH on amylase activity, five identical plastic cups were labeled
as follows: a. Water, b. Water + Sugar, c. Water + Starch, d. Saliva + Starch, and e. Saliva
+ Acid + Starch. Each cup was then filled with 10 ml of water.

Four spits of saliva were added to the cups labeled "Saliva" and "Saliva + Starch," followed
by gentle swirling to mix. Ten drops of vinegar were added to the "Saliva + Acid" cup, and
2 pinches of sugar were added to the "Water + Sugar" cup. Finally, 2 pinches of starch
were added to all cups containing "Starch," and the cups were swirled to mix.

The cups were then allowed to sit for 15-25 minutes, during which time the amylase
enzyme in the saliva would break down the starch. After 25 minutes, 3 drops of betadine
were added to each cup. Betadine reacts with starch, turning it blue-black. Therefore, any
cups that remained blue-black indicated the presence of undigested starch, suggesting
that amylase activity was inhibited.

Figure 3.8. Shows the materials needed for the Figure 3.9. Shows the effect of pH on enzyme
experiment such as 5 labeled plastic activity of 5 different labeled cups.
cups, vinegar, cornstarch, sugar,
betadine, and saliva.

D. Effect of Concentration on Enzyme Activity (Hydrogen Peroxide and Catalase)

Materials:
Yeast 1 Graduated cylinder (50ml)
Water Hydrogen peroxide
Graduated cylinder Dropper
3 beakers (100 ml) Timer
3 plastic cups
D1. Experiment Preparation

To investigate the effect of concentration on enzyme activity, three solutions were prepared.
Solution A contained 4 pinches of yeast in 26 ml of water. Solution B was created by adding
1 ml of solution A to 24 ml of water. Finally, solution C was made by adding 5 ml of solution
A to 20 ml of water.

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 Three uncovered 100-ml beakers were labeled A, B, and C, and each contained
approximately 15 ml of hydrogen peroxide using a graduated cylinder. Then 15 drops of
each solution were quickly added to the corresponding beaker. The reaction was observed
for a few minutes, focusing on the formation of bubbles on the surface of the hydrogen
peroxide.

The order in which bubbles appeared and their frequency were recorded for each solution,
allowing for a comparison of enzyme activity based on the concentration of the catalase
enzyme in the yeast solutions.

Figure 3.10. Shows the adding of Figure 3.11. Shows the three solutions: cup A
corresponding amounts of yeast in contains of 4 pinches of yeast in 26 ml
Cup A. of water, cup B contains 1 ml of
solution A to 24 ml of water, and cup C
contains 5 ml of solution A to 20 ml of
water

Figure 3.12. Shows three 100-ml beakers Figure 3.13. Shows the reaction of the effect of
labeled A, B, and C, and each concentration on hydrogen and
contained approximately 15 ml of catalase activity in the solutions of cup
hydrogen peroxide. A, B, and C.
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 RESULTS AND DISCUSSION

Table 3.1 Catalase

OBSERVATIONS

Fresh potato tuber strips in Produced a significant amount of oxygen

Hydrogen Peroxide bubbles indicating high catalase activity

Boiled potato tuber in Produced little to no oxygen bubbles, indicating low catalase
activity
Hydrogen Peroxide

In the fresh potato tuber strips, a significant production of oxygen gas bubbles was observed,
indicating high catalase activity. This suggests that the catalase enzyme in the fresh potato cells is intact
and fully functional, efficiently breaking down hydrogen peroxide into water and oxygen. In contrast, the
boiled potato tuber strips produced little to no oxygen bubbles, indicating significantly reduced or absent
catalase activity. This is likely due to the denaturation of the catalase enzyme caused by the high
temperature during boiling, which disrupts its structure and prevents it from effectively catalyzing the
breakdown of hydrogen peroxide.

Catalase enzyme is a vital enzyme that plays a crucial role in the survival of plants. Hydrogen
peroxide is a highly toxic substance, which is highly reactive and can induce deleterious oxidations on lipids,
carbohydrates, and proteins (Mizuno et al., 1998). In plant cells, hydrogen peroxide can form during
photosynthesis, respiration, and photorespiration, this stresses the need for antioxidant mechanisms in
plants (Slesak et al., 2007). As a response, some plants have enzymes that detoxify hydrogen peroxide,
an example enzyme is catalase which is abundantly found in potato tissues (Cascio, 2013). This finding
suggests that catalase is naturally found in fresh potatoes, indicating that both must be present in fresh
potato tubers, both boiled and unboiled.

Therefore, presence or absence of the catalase reaction can be attributed to activation of the
enzyme. The catalase reaction was seen to be active in the unboiled potato strip, while it was absent in the
boiled potato strip. This is supported as the presence of a catalase reaction can be determined by gas
evolution in the hydrogen peroxide solution, which is due to the formation of oxygen bubbles from
decomposition of hydrogen peroxide (Iwase et al., 2013). The absence of reaction in the boiled potato strips
can be attributed to the effect of high temperatures due to exposure from boiling. Catalase activity has an
optimum temperature of 37°C, as temperatures deviate from this the rate of reaction lowers. Eventually this
leads to inactivity in very low and high temperatures, catalase has been observed to be inactive specifically
at 45°C as it breaks intramolecular bonds and distorts the active site of the enzyme (Lee, 2020).

These findings support the hypothesis that temperature has a significant effect on enzymatic
reactions. More specifically, the observations suggest that catalase under optimal temperature is highly
active in fresh potato tissue, but the enzyme is denatured and inactivated by boiling, which prevents it from
functioning properly.

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Table 3.2 The Bromelain Enzyme and Effect of heating on Bromelain.

TYPE OF RESULTS
FRUIT

Apple No significant activity was observed indicating that apple does not contain
bromelain or other proteolytic enzyme

Orange No significant activity was observed indicating that orange does not contain bromelain
or other proteolytic enzyme

Pineapple Bromelain was highly active, breaking down proteins into smaller peptides and amino
acids

Heated Apple No significant activity was observed indicating that apple does not contain bromelain or
other proteolytic enzyme

Heated No significant activity was observed indicating that apple does not contain bromelain or
Orange other proteolytic enzyme

Heated No significant activity was observed indicating that the bromelain enzyme was
Pineapple disrupted upon heating the pineapple in the microwave oven.

In the case of the fresh apple and orange, no significant effect on the gelatin was noted and no
proteolytic activity was detected, indicating that it does not contain bromelain or any other proteolytic
enzymes capable of breaking down proteins. Meanwhile, iIn the fresh pineapple, significant proteolytic
activity was observed when placed in gelatin, resulting in a noticeable reduction in the firmness of the
gelatin. This confirms that pineapple contains active bromelain, which is highly effective in catalyzing protein
breakdown.

In contrast, the heated pineapple sample, no proteolytic activity was detected when placed in gelatin,
and the gelatin remained intact, maintaining its structure and firmness, showing no significant change. This
lack of activity indicates that the bromelain enzyme, which is responsible for breaking down proteins in fresh
pineapple, was denatured upon heating. Similarly, heating the apple and orange similarly showed no
change in activity, simply this is because there were no proteolytic enzymes present to begin with that can
be affected by heat.

Bromelain is an enzyme found in cells which is vital for protein digestion. Particularly, it is a sulfhydryl
proteolytic enzyme, which catalyzes the breakdown of proteins into amino acids. More importantly, the
importance of this protein has been observed in the protection of pineapple plants, especially during their
development, maturity, development, and ripening processes (Agrawal et al., 2022). Commercial gelatin is
a purified protein which is particularly rich in collagen, as a result the peptide bonds in collagen are
hydrolyzed in the presence of bromelain (Glider & Hargrove, 2002).

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This can be observed in the experiment through the liquification of the gelatin as it fails to stay put and
remain solid. These findings supports the observation that bromelain is present in the pineapple fruit and
absent in apple and orange fruits, as gelatin was observed to liquify only in the pineapple. This finding is
supported as pineapple fruits and even stems are common natural sources of bromelain, in contrast apple
and orange fruits do not produce the bromelain enzyme as observed in the experiment (NCCIH, 2020).

In contrast, though bromelain is also present in the heated pineapple, no sign of liquification on the
gelatin was observed. The inactivity of the enzyme can be attributed to the effect of heating the pineapple.
Pineapple bromelain activity has been observed to be optimal around 40°C, going above 50°C the rate of
reaction rapidly decreases until almost complete loss of activity at 80°C (Jutamongkon & Charoenrein).
More specifically, this is due to the denaturation process in structures in enzymes, wherein high
temperatures break the hydrogen and ionic bonds present in the protein therefore altering the shape of the
active site (Bartee & Brook, 2019). In relation to this, bromelain in canned pineapple products were
inactivated due to the typical procedures involving heat during simmering and vacuuming, this emphasizes
the use of fresh pineapple and other fresh fruits in the study.

These findings further support the hypothesis that temperature has a significant effect on enzymatic
reactions. More specifically, the observations suggest that bromelain under optimal temperature is highly
active in fresh pineapple fruits, but the enzyme is denatured and inactivated once heated, which prevents
it from functioning properly.

Table 3.3 Effect of pH on enzyme activity (Starch and Amylase).

CUP ACTUAL RESULTS

Water Orange-Brown Coloration

Water + Sugar Orange-Brown Coloration

Water + Starch Dark Blue-Black Coloration

Saliva + Starch Orange-Brown Coloration

Saliva + Acid + Starch Dark Blue-Black Coloration

This water shows no reaction. Indicating that water alone does not have any effect on starch or
amylase activity. There is no starch or other reactants that would cause a color change with iodine, so the
solution maintains a neutral orange-brown color (the color of iodine in solution). Similar to the water, the
presence of sugar in water does not trigger any starch breakdown or interaction with iodine. Sugar does
not react with iodine, so the orange-brown coloration persists. This confirms that sugar has no impact on
starch in terms of iodine reactivity or enzyme activity.

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 When iodine is added to a starch-containing solution, it forms a complex that produces a blue-black
coloration. This result indicates the presence of starch in the solution. This result confirms that the starch
is present and unaltered in the absence of enzymes or other reactants.

In the Saliva + Starch solution, Blue-black coloration was observed, indicating that the starch remains
intact, as it still reacts with iodine. This is due to the presence of the saliva which contains the enzyme
amylase, that breaks down starch into simpler sugars. This suggests that the conditions (pH) in the
experiment may not have been optimal for amylase activity. If the enzyme is not active, starch remains
unbroken, and the iodine test will show the blue-black color, indicating starch is still present.

The orange-brown coloration observed in Saliva+Acid+Starch solution indicates that no starch is

present in this sample. Saliva contains amylase, which should break down starch, but the addition of acid
(vinegar) likely deactivated the amylase. Acidic environments can denature enzymes, changing their shape
and rendering them unable to catalyze reactions.

Amylase derived in human saliva functions as a digestive enzyme for carbohydrates, specifically it
breaks down starch by hydrolysis into smaller sugar units in the form of maltose (Peyrot des Gachons &
Breslin, 2016). In conjunction, it can be implied that the activity of the amylase enzyme can be observed by
the presence of starch, as active amylase successfully breaks down starch while inactive amylase doesn’t
break down the starch. The presence of starch then can also be determined through colorimetric reactions
such as its reactions with iodine. Commercial betadine contains iodine which can react with starch to form
an iodine-starch complex, more specifically this describes iodine bounded to the helical structure of amylase
in the starch which produces a deep-blue color (Pesek et al., 2022).

In order to test this iodine is added to control samples such as solutions containing (a) water, (b)
water + sugar, and (c) water + starch. The control samples serve the role of being the reference points for
reactions without experimental treatment, in order to better isolate the effect of pH on amylase activity. From
the observations, iodine forms a dark blue-black color in the presence of starch in the water + starch
solution, which is supported from the previous finding. While the natural orange-brown color of betadine is
retained in the water and water + sugar solution. The experimental samples include (a) saliva + starch and
(b) saliva + acid + starch solutions, with saliva containing active amylase enzymes. These experimental
samples test for the activity of amylase enzymes in different pH conditions, specifically the water + starch
solution represent neutral conditions while water + acid + starch solution represent acidic conditions.

Findings of the study suggest that amylase activity is pH dependent, this is due to the observed
differences of activity in neutral and acidic solutions as indicated by the difference in their reactions with
iodine. In another study, it has also been observed that salivary amylase works best in a pH range from 6.9
- 7.0 but it is inactivated by acidic denaturation as acidic conditions disrupts hydrophobic interactions and
protonation of amino acids, which alters the structure of the enzyme (Akinfemiwa et al., 2022; Singh et al.,
2015). It can also be implied that other acidic substances would inactivate the amylase in saliva, such as
hydrochloric acid found naturally in the stomachs of our body. In contrast, the acidic conditions due to the
strong acid present allow for different enzymes that work best in the stomach. An enzyme for example
includes pepsin which is a pepsinogen that is activated once introduced to the acidic environment of the
stomach (Heda et al., 2023).

These findings further support the hypothesis that pH has a significant effect on enzymatic reactions.
More specifically, the observations suggest that amylase activity is optimal at neutral pH levels, while the
enzyme denatures at acidic pH levels.

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 Table 3.4 Effect of concentration on Enzyme Activity (Hydrogen Peroxide and Catalase)

CATALASE SOLUTION ORDER OF REACTION

A 1st, with most bubble produced

B 3rd, with least bubbles produced

C 2nd, more bubbles than B, but less than A

Solution A produced the most oxygen bubbles, having the highest enzyme activity. It indicates that
catalase in this solution was most efficient in breaking down hydrogen peroxide into oxygen and water. This
suggests that Solution A had the highest concentration of catalase or the most optimal conditions (e.g.,
temperature or pH) for catalase activity.

Solution B produced the least quantity of bubbles, indicating the lowest enzyme activity. This could
be due to the lowest concentration of catalase or less favorable conditions for enzyme function (such as
suboptimal temperature, pH, or enzyme denaturation).

Solution C showed intermediate enzyme activity. It produced more bubbles than B, but fewer than A,
indicating a moderate concentration of catalase. The reaction rate was higher than in Solution B, but not as
fast as in Solution A, suggesting that the enzyme concentration was higher than in B but lower than in A, or
that other reaction conditions (e.g., pH, temperature) were less optimal than in A.

As described earlier, the three catalase solutions had varying catalase concentrations. More
specifically, solution A has the highest catalase concentration, followed by solution C, then lastly solution
B. This is supported by the order and frequency of bubble formation observed in the experiment as the
bubbles formed indicate the activity of the catalase enzyme. Notably, this also implies that catalase is active
in all solutions, though the rate of reaction varies according to their concentration. This is supported by the
basic principle in enzyme kinetics wherein there is a directly proportional relationship between enzyme
concentration and rate of reaction as more enzymes are available to catalyze the reaction ().

Catalase decomposes hydrogen peroxide into water and oxygen, therefore the bubbles formed
during the reaction are due to the oxygen gas produced. The confirmatory test for the presence of oxygen
can be done by a glowing splint test wherein the presence of oxygen can be determined if the glowing splint
is reignited (Carolina Knowledge Center, 2022). With the formation of oxygen, this can be utilized in the
context of medicine. Given that pathogenic bacteria causes gangrene is anaerobic, the application of
hydrogen peroxide on a wound can lessen the risk of gangrene as gangrene-causing bacteria is unable to
tolerate the produced oxygen cause from the applied hydrogen peroxide. This emphasizes the potential
role of catalases as preventive measures against anaerobic pathogens.

These findings further support the hypothesis that enzyme concentration has a significant effect on
enzymatic reactions. More specifically, the observations suggest that catalase’s rate of activity increases
as the catalase concentration also increases.

To conclude, enzymes as biological catalysts are dependent and sensitive to different factors and conditions
present. As demonstrated from the study, factors such as temperature, pH, and enzyme concentration can
significantly affect the activity of enzymes, it can inactivate and even speed up or slow down the rate of

12
reaction. More specifically, it can be understood that enzymes tend to work effectively under optimal
temperature and pH ranges, deviating from this can slow down or even inactivate them, while increasing
enzyme concentration generally speeds up the rate of reaction. This emphasizes the sensitive balance in
considering the optimal activity of enzymes.

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15
 Distribution of work:

Results

Pareja, Ma. Micaela V.

Abstract and Introduction

Peñaranda, Marcus Arveinzl O.

Discussion and Conclusion

Uy, Frederick

Materials and Methods

Visperas, Justine May G.

Group 2 - BS BIOLOGY lllA (SET B)