Enzyme Activity
Dial up temperature, pH, substrate, and enzyme concentration and watch reaction rate rise and fall — matches the school experiment on how temperature and pH affect enzymes, with a real Michaelis-Menten curve and a reaction-progress colour change.
What you can adjust
- Enzyme
- 0 – 2
- Substrate concentration
- 0 – 50 mM
- Enzyme concentration
- 0.1 – 2 x
- Temperature
- 0 – 80 °C
- pH
- 1 – 14
Picks the enzyme's illustrative Km and optimum pH (every preset shares the same ~37 °C optimum temperature — ordinary body temperature). Amylase and catalase work best near neutral pH; pepsin works best in the strongly acidic stomach.
Concentration of the substrate the enzyme is acting on. At low concentration the rate rises roughly in proportion to this; once it is well above the enzyme's Km, adding more barely speeds the reaction up further (the enzyme is saturated).
Relative amount of enzyme present (1.0x is a standard amount). The maximum possible rate (Vmax) scales directly with this — twice the enzyme, twice the top speed of the reaction.
Reaction temperature. Activity rises with temperature up to the enzyme's optimum, then falls sharply above it as the enzyme denatures and permanently loses its shape. Marked as a highlight point on the traced curve.
Reaction pH. Activity peaks at the enzyme's own optimum pH and falls off on both sides as the enzyme's shape (and its active site) is disrupted.