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Topic 4

Biological molecules and enzymes

IB MYP Biology · Metabolism · MYP Years 4–5

🔒 Printable worksheet for this topic (members) →

Living things are built from a small set of large molecules — carbohydrates, proteins and lipids — and run by enzymes, the protein catalysts that make the chemistry of life fast enough to keep us alive at body temperature.

🎯What you need to be able to do

  • Name the chemical elements and building blocks of carbohydrates, proteins and lipids.
  • Describe the food tests for starch, reducing sugar, protein and fat.
  • Explain what an enzyme is and how the lock-and-key model works.
  • Explain the effect of temperature and pH on enzyme activity, including denaturation.
  • Interpret graphs of enzyme activity and design enzyme investigations.

🍞The molecules of life

MoleculeElementsMade fromRoles
carbohydratesC, H, Osimple sugars (e.g. glucose) join to form starch, glycogen and celluloseenergy source (glucose); storage (starch in plants, glycogen in animals); structure (cellulose walls)
proteinsC, H, O, N (some S)amino acids, about 20 kinds, in a specific orderenzymes, antibodies, haemoglobin, muscle, hormones such as insulin
lipids (fats and oils)C, H, Oglycerol + three fatty acidsenergy store (twice as much per gram as carbohydrate), insulation, cell membranes

Large molecules like starch and proteins are polymers: long chains of smaller units. The order of amino acids decides how a protein folds, and its shape decides its function. Water is also vital: it makes up about 70% of a cell, dissolves substances so they can react and be transported, and helps regulate temperature.

🧪Food tests

Test forMethodPositive result
starchadd iodine solutionorange-brown → blue-black
reducing sugar (e.g. glucose)add Benedict’s solution, heat in a water bath (~80 °C)blue → green, yellow or brick-red (more sugar = further along)
proteinadd biuret solutionblue → purple/lilac
fatshake with ethanol, then pour into watercloudy white emulsion

🔑Enzymes

Enzymes are biological catalysts: proteins that speed up chemical reactions in living things without being used up. Without them, reactions such as digesting starch or copying DNA would be far too slow at 37 °C. Each enzyme has an active site, a region with a precise shape that fits only one type of molecule, its substrate.

The lock-and-key model in three steps: a substrate molecule with a shape complementary to the enzyme's active site; the substrate fits into the active site forming an enzyme–substrate complex; the products leave and the enzyme is unchanged and can be used again.
Only a substrate with the complementary shape fits the active site. The enzyme is reused.

In the lock-and-key model, the substrate fits the active site like a key in a lock, forming an enzyme–substrate complex. The reaction happens, the products leave, and the enzyme is free to catalyse again. Because each active site fits one substrate, enzymes are specific: amylase breaks down starch but not protein.

🌡️Temperature and pH

Two graphs of rate of enzyme activity. Against temperature: the rate rises gradually to a peak at the optimum of about 37 degrees Celsius, then falls steeply to zero by about 60 degrees as the enzyme is denatured. Against pH: pepsin has a peak at pH 2, while amylase has a peak at about pH 7.
Each enzyme has an optimum temperature and an optimum pH.
  • Temperature: as temperature rises, molecules move faster and collide more often, so the rate increases up to the optimum (about 37 °C for human enzymes). Above it, the enzyme’s bonds start to break and the active site changes shape: the substrate no longer fits. The enzyme is denatured — a permanent change. At low temperatures enzymes are inactive but not denatured, which is why fridges slow food decay.
  • pH: each enzyme has an optimum pH. Pepsin in the acidic stomach works best at about pH 2; amylase in the mouth and small intestine at about pH 7. Too far from the optimum and the active site changes shape, denaturing the enzyme.

✏️Worked example: amylase and temperature

A student mixes starch and amylase at different temperatures and records the time until the mixture no longer turns iodine blue-black. Results: 20 °C 240 s; 30 °C 120 s; 40 °C 60 s; 50 °C 150 s; 60 °C no end point after 600 s. Calculate the rate at 40 °C and explain the pattern.

Rate = 1 ÷ time = 1 ÷ 60 = 0.017 s−1 (the shorter the time, the higher the rate).

Pattern: from 20 to 40 °C the time halves with each 10 °C rise: molecules have more kinetic energy, so there are more frequent successful collisions between starch and active sites. The optimum is near 40 °C. At 50 °C the enzyme begins to denature, and at 60 °C it is fully denatured: the active site has changed shape so starch is not broken down at all.

Improving the conclusion: the true optimum could be anywhere between 30 and 50 °C. Repeat with 2 °C steps in that range to find it more precisely.
The trap: saying the enzyme was “killed”. Enzymes are molecules, not living things; they are denatured.

🌎Science in context: enzymes in industry

Enzymes are used to make biological washing powders work at low temperatures (saving energy), to turn starch into sugar syrups, to soften leather, and to produce lactose-free milk. Tempeh and other fermented foods depend on the enzymes of fungi. Industrial enzymes save energy because they work at moderate temperatures, but they must be kept in their narrow working range of temperature and pH.

🧠Quick check

1. Which element is found in proteins but not in carbohydrates or lipids?

Nitrogen (and sometimes sulfur).

2. Describe the test for protein.

Add biuret solution to the food sample (in solution); a colour change from blue to purple shows protein.

3. What is an active site?

The region of an enzyme with a specific shape into which its substrate fits.

4. Why can an enzyme only catalyse one type of reaction?

Its active site has a specific shape that is complementary to only one substrate (enzymes are specific).

5. What happens to an enzyme at 70 °C?

It is denatured: bonds holding its shape break, the active site changes shape and the substrate no longer fits. The change is permanent.

6. Why does pepsin work in the stomach but not in the small intestine?

Pepsin’s optimum pH is about 2, matching the acidic stomach. The small intestine is neutral to slightly alkaline, which changes pepsin’s active site.

📝Worksheet

Test yourself on the whole topic with a printable worksheet: questions for all four criteria, from recall to a design task, a data-analysis question and a short reflection, with a full mark scheme.

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