K327 / K328 / 2027

Chapter summary

Biological molecules, at a glance

Scan the key ideas, or hide the answers and try to recall them.

01

Carbohydrates, fats and proteins

What does each group contribute to a living organism?

Key idea and reminders

Carbohydrates provide an immediate energy source, fats provide insulation and long-term energy storage, and proteins support cell growth and repair.

  • Carbohydrates: an immediate energy source.
  • Fats: long-term energy storage and insulation.
  • Proteins: growth and repair of cells.

Keep in mind: Insulation reduces heat loss. Energy release in respiration and reduced transfer of heat to surroundings are different processes.

02

Building larger molecules

How can a few small units make very different large molecules?

Key idea and reminders

Glucose units build starch, glycogen and cellulose. Amino acids build polypeptides and proteins. Glycerol and fatty acids build fats.

  • Starch, glycogen and cellulose all use glucose units, joined in different arrangements.
  • Amino acid sequence affects the shape and function of a protein.
  • A fat molecule is assembled from glycerol and fatty acids; it is not a long chain of glucose.

Keep in mind: Proteins are made from amino acids. Fats are made from glycerol and fatty acids. Glucose builds starch, glycogen and cellulose.

03

Testing for starch and reducing sugars

What does a colour change actually show?

Key idea and reminders

Iodine solution tests for starch. Heated Benedict's solution tests for reducing sugars. A result identifies what the test detects, not every carbohydrate present.

  • Starch: iodine in potassium iodide changes from yellow-brown to blue-black.
  • Reducing sugar: Benedict's solution is heated in a water bath; a coloured precipitate is a positive result.
  • A negative Benedict's test does not prove that a food contains no carbohydrate.

Keep in mind: Benedict's test detects reducing sugars, not every carbohydrate. Starch may still be present, so choose a separate appropriate test.

04

Testing for proteins and fats

How do you distinguish a colour change from an emulsion?

Key idea and reminders

Biuret solution gives a violet or purple colour with protein. The ethanol emulsion test gives a cloudy white emulsion when fat is present.

  • Protein: add biuret reagent; blue changes to violet or purple.
  • Fat: mix with ethanol, then add the ethanol extract to water; a cloudy white emulsion indicates fat.
  • Keep ethanol away from flames and heat sources. Food-test samples must not be tasted.

Keep in mind: The fat test produces a cloudy white emulsion after ethanol extraction and addition to water. Benedict's solution is used with heating to test for reducing sugars.

05

How enzymes speed up reactions

Why does one enzyme act on a particular substrate?

Key idea and reminders

A complementary substrate fits an enzyme active site, forms a temporary complex and is changed into products. The enzyme can then work again.

  • Enzymes are biological catalysts: they increase reaction rate without being used up.
  • The lock-and-key model links a complementary active-site shape to enzyme specificity.
  • The enzyme-substrate complex is temporary; products leave and the enzyme can be reused.

Keep in mind: The substrate changes into products, while the enzyme remains available to catalyse another reaction.

06

Temperature and enzyme activity

Why does warming help only up to a point?

Key idea and reminders

Warming initially increases productive collisions. Above the optimum, denaturation changes the active site and reduces the rate. Cooling usually slows activity without denaturing the enzyme.

  • Below the optimum: higher temperature increases particle movement and productive collisions.
  • Excessive heat changes enzyme shape; the substrate fits less well or not at all.
  • For the same endpoint, relative rate can be compared using 1/time. Keep other variables constant.

Keep in mind: Low temperature can slow collisions while leaving the active site intact. A low rate alone does not establish denaturation; the cause and conditions matter.

07

pH and enzyme activity

Why can an enzyme work well in the stomach but poorly in the mouth?

Key idea and reminders

Each enzyme has a suitable pH range. Moving away from its optimum can change the active site and reduce activity; extreme pH can denature it.

  • Different enzymes can have different optimum pH values.
  • A buffer keeps the reaction mixture near a chosen pH.
  • When changing pH, hold temperature, enzyme concentration and substrate concentration constant.

Keep in mind: Enzymes have different pH ranges. Some stomach enzymes are adapted to acidic conditions. Explain the response of the particular enzyme using its optimum and active site.

Can you explain a new example?

Use the ideas from this chapter to explain a result in your own words.

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