DATA TABLE

pH ENZYME ACTIVITY
 When 2ml of 0.4% HCl is mixed with 1ml
catechol, the result is colorless.
 When 1mL of potato extract is added to
1 0.4%hcl, the color is white with a small orange
tint, and after 15 minutes of boiling, the color
becomes white/cream.

 When 2ml of 0.1% lactic acid is mixed with

1ml catechol, the result is colorless.
 When 1ml of potato extract is added to 0.1%
lactic acid, the color is white with a small
5 orange tint, and after 15 minutes of boiling, the
color becomes white/cream.
 When 2ml of distilled water (DH2O) is mixed
with 1ml catechol, the result is colorless.
 When 1ml of potato extract is added to 2ml of
DH20, the color is light orange, and after 15
7 minutes of boiling, the color becomes light
peach.
 When 2ml of sodium carbonate (Na2Co3) is
mixed with 1ml catechol, the result is
colorless.
 When 1ml of potato extract is added to 2ml of
9 Na2Co3, the color is yellowish, and after 15
minutes of boiling, the color becomes
yellowish brown.

GRAPH
QUESTIONS FOR RESEARCH
1. WHAT ARE THE OPTIMUM CONDITIONS FOR ENZYME ACTIVITY IN THE
HUMAN ACTIVITY?
- Most enzymes in the human body work best at around 37°C – body temperature. At lower
temperatures, they will still work but much more slowly. Similarly, enzymes can only function in a
certain pH range (acidic/alkaline). Enzymes play a huge part in the day-to-day running of the
human body. By binding to and altering compounds, they are vital for the proper functioning of the
digestive system, the nervous system, muscles, and much more.

2. GIVE OTHER FACTORS WHICH INFLUENCE ENZYME ACTIVITY AND STATE

THE EFFECT OF EACH FACTOR.
5 FACTORS AFFECTING ENZYME ACTIVITY

1. Enzyme Concentration- Transient bonds formed between enzymes and their substrates
catalyze processes by lowering activation energy and stabilizing the transition state. Given an
abundance of substrates and appropriate cofactors, enzymatic processes with greater enzyme
concentrations will approach equilibrium before those with lower enzyme concentrations. Simply
said, more enzyme molecules are available to digest the substrate when the enzyme
concentration is higher. Because of the high quantities of enzyme-substrate complex, the reaction
has a faster initial catalytic rate, giving it a head start in the shift toward reactant-product
equilibrium.
2. Substrate Concentration- The enzyme catalytic activity occurs when a geometrically and
electronically complementary substrate can access the enzyme’s catalytic or active site. There,
the active residues transiently bond with the substrate, catalyzing the transformation of the
substrate into a product. Thus, the more substrate-occupied active sites, the higher the catalytic
activity and the faster the shift toward enzyme-product equilibrium.

3. pH Value- The amino acids determine substrate selectivity and limit enzyme activity to a certain
pH range. Most enzymes perform best in slightly acidic or basic environments. However, a few
enzymes are native to extremely acidic or basic environments, and so are most active in these
pH ranges.

4. Temperature- As the reactants gain kinetic energy, a minor rise in temperature can accelerate
the reaction rate. Significant temperature excursions from the ideal temperature, on the other
hand, drastically limit enzyme activity. Extremely high temperatures can cause the intramolecular
bonds and enzyme structure to be destroyed, rendering the enzyme irreversibly inactive. Low
temperatures reduce the system's kinetic energy and thus the rate of reaction. As the
temperature falls below the ideal level, enzyme activity decreases. In contrast to high
temperatures, low temperatures do not always result in permanent enzyme denaturation, and
enzyme function can be restored if the temperature increases to the optimum range.

5. Inhibitor- Inhibitors can bind to the enzyme or its substrate and inhibit ongoing enzymatic
activity, preventing subsequent catalytic steps. When inhibitors make strong bonds to the
enzyme's functional group, the effect on enzyme activity is irreversible, rendering the enzyme
irreversibly inactive. Reversible inhibitors, as opposed to irreversible inhibitors, only render
enzymes inactive when attached to the enzyme. Competitive inhibitors compete with substrates
for binding to the enzyme functional group residues at the catalytic sites. Other forms of inhibitors
bind to the non-substrate binding allosteric site rather than the catalytic site. If an inhibitor binds to
the enzyme concurrently with the enzyme-substrate binding, it is non-competitive. If an inhibitor
binds only to a substrate-occupied enzyme, it is uncompetitive.

3. WHAT DOES SALIVA CONTAIN? WHAT IS IT’S OPTIMUM PH? HOW DOES IT
FUNCTION?
- Salivary amylase, found in human saliva, is an enzyme used to hydrolyze starch molecules.
And its optimum pH ranges from 6 to 7. The digestive functions of saliva include moistening food,
and helping to create a food bolus, so it can be swallowed easily. Saliva contains the enzyme
amylase that breaks some starches down into maltose and dextrin. Thus, digestion of food occurs
within the mouth, even before food reaches the stomach.

4. COMPARE AND CONTRAST PEPSIN AND TRYPSIN AS TO LOCATION OF

DIGESTION AND HYDROLYSIS PRODUCT?
- Pepsin is the chief digestive enzyme in stomach, which is produced by the gastric gland in
stomach and is a component of gastric juice, while trypsin in produced by the pancreas and is a
component of pancreatic juice. The optimum pH for pepsin activity is 1.8, while trypsin works best
in alkaline pH (pH 7.5-8). Pepsin hydrolyzes peptide bonds between large hydrophobic amino
acid residues, whereas trypsin hydrolyzes peptide bonds at the C-terminal side of lysine or
arginine. Pepsin acts on proteins and converts them into peptones, while trypsin converts
peptones into polypeptides.

REFERENCES:
Enzymes: Function, definition, and examples (medicalnewstoday.com)

Factors That Affects Enzyme Activity – Conduct Science

Factors Affecting Enzyme Activity: 6 Factors (biologydiscussion.com)

Enzymatic Activity of Salivary Amylase Formal Report - PDFCOFFEE.COM

What is the difference between trypsin and pepsin? | AAT Bioquest