Skip to main content
EnglandCombined ScienceSyllabus dot point

How do enzymes speed up the reactions of metabolism, and why do temperature and pH change how fast they work?

Enzymes as biological catalysts, the lock and key model and the active site, the effect of temperature, pH and substrate concentration on enzyme activity, denaturing, and the breakdown of carbohydrates, proteins and lipids by digestive enzymes.

A focused answer to the OCR Gateway GCSE Combined Science A topic B1 work on enzymes, covering enzymes as biological catalysts, the lock and key model, the effects of temperature, pH and concentration, denaturing, and the digestive enzymes amylase, protease and lipase.

Generated by Claude Opus 4.89 min answer

Reviewed by: AI editorial process; not yet individually human-reviewed

Have a quick question? Jump to the Q&A page

Jump to a section
  1. What this topic is asking
  2. Enzymes as biological catalysts
  3. Temperature, pH and concentration
  4. Digestive enzymes

What this topic is asking

OCR wants you to explain that enzymes are biological catalysts, describe the lock and key model, explain how temperature, pH and substrate concentration change the rate, define denaturing, and describe how digestive enzymes break down the large food molecules.

Enzymes as biological catalysts

Living cells run thousands of chemical reactions, together called metabolism, and most would be far too slow at body temperature without enzymes. Because an enzyme is not used up, one molecule catalyses the reaction over and over again. The lock and key model explains the specificity: the substrate fits into the active site like a key fits a lock, the enzyme holds the substrate while the reaction happens, and the products are then released, leaving the active site free again. A given enzyme only works on a substrate whose shape matches its active site, which is why amylase breaks down starch but not protein.

Temperature, pH and concentration

The rate of an enzyme reaction depends on the conditions:

  • Temperature. Raising the temperature gives molecules more energy, so the enzyme and substrate collide more often and with more energy, and the rate rises up to the optimum (about 3737 degrees Celsius for many human enzymes). Above the optimum the enzyme denatures: the bonds holding its shape break, the active site changes shape, and the substrate no longer fits, so the rate falls sharply.
  • pH. Each enzyme has an optimum pH. Moving away from it changes the active site shape and slows the reaction; a large change denatures the enzyme. Stomach protease (pepsin) works best in acidic conditions, while amylase in the mouth and small intestine prefers a neutral or slightly alkaline pH.
  • Substrate concentration. Increasing the substrate concentration speeds the reaction up because collisions are more frequent, until all the active sites are working as fast as they can, after which the rate levels off.

Digestive enzymes

Large food molecules are too big to be absorbed, so digestive enzymes break them into small soluble molecules. Amylase (made in the salivary glands and pancreas) breaks starch into sugars such as maltose. Proteases (such as pepsin in the stomach) break proteins into amino acids. Lipase (made in the pancreas) breaks lipids (fats and oils) into fatty acids and glycerol. Bile, made in the liver and stored in the gall bladder, is not an enzyme but it neutralises stomach acid and emulsifies fats into small droplets, giving a larger surface area so lipase works faster. The small soluble products are then absorbed into the blood across the wall of the small intestine.

Exam-style practice questions

Practice questions written in the style of OCR exam questions on this dot point, with worked answer explainers. The year tag is the paper they imitate, not the source.

OCR 20196 marksExplain how temperature affects the rate of an enzyme-controlled reaction, including what happens above the optimum temperature.
Show worked answer →

A Biology Paper 1 six-mark extended response, marked on a levels basis. Reward a logical chain: as temperature rises from cold, the enzyme and substrate molecules move faster and collide more often with enough energy, so the rate of reaction increases; the rate is highest at the optimum temperature (about 3737 degrees Celsius for many human enzymes). Above the optimum, the increasing heat energy makes the enzyme's structure vibrate and break the bonds holding its shape, so the active site changes shape and the substrate no longer fits. This is denaturing, and it is permanent, so the rate falls and eventually stops. Top-level answers link the active site shape to the substrate fit, use the word denatured correctly, and note that enzymes are proteins, not living things, so they are denatured rather than killed.

OCR 20214 marksA student investigates how pH affects the activity of amylase. Describe a method they could use and name the product they would test for.
Show worked answer →

A required-practical style question on enzyme action. Reward a clear method: mix amylase with starch in solutions buffered to a range of pH values, keep them in a water bath at a constant temperature, and at set times remove a drop and test it with iodine solution. The amylase breaks starch down into sugar, so the iodine stops turning blue-black (it stays orange-brown) when the starch has gone, and the time taken to reach this point measures the rate. Markers credit controlling temperature and enzyme/starch volumes, using a buffer to set pH, and testing with iodine; full marks need the link from faster starch breakdown to a shorter time.

Related dot points

Sources & how we know this