The document discusses various factors affecting enzyme activity, including enzyme and substrate concentration, temperature, pH, product concentration, activators, time, and light exposure. It explains the relationship between substrate concentration and reaction velocity, the significance of the Michaelis-Menten constant (Km), and the optimal conditions for enzyme activity. Additionally, it highlights how temperature and pH influence enzyme performance, with specific examples of enzymes that thrive under different conditions.
The document discusses various factors affecting enzyme activity, including enzyme and substrate concentration, temperature, pH, product concentration, activators, time, and light exposure. It explains the relationship between substrate concentration and reaction velocity, the significance of the Michaelis-Menten constant (Km), and the optimal conditions for enzyme activity. Additionally, it highlights how temperature and pH influence enzyme performance, with specific examples of enzymes that thrive under different conditions.
The document discusses various factors affecting enzyme activity, including enzyme and substrate concentration, temperature, pH, product concentration, activators, time, and light exposure. It explains the relationship between substrate concentration and reaction velocity, the significance of the Michaelis-Menten constant (Km), and the optimal conditions for enzyme activity. Additionally, it highlights how temperature and pH influence enzyme performance, with specific examples of enzymes that thrive under different conditions.
The document discusses various factors affecting enzyme activity, including enzyme and substrate concentration, temperature, pH, product concentration, activators, time, and light exposure. It explains the relationship between substrate concentration and reaction velocity, the significance of the Michaelis-Menten constant (Km), and the optimal conditions for enzyme activity. Additionally, it highlights how temperature and pH influence enzyme performance, with specific examples of enzymes that thrive under different conditions.
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Factors affecting
enzyme activity 1. Concentration of enzyme
As the concentration of the enzyme
is increased, the velocity of the reaction proportionately increases. 2. Concentration of substrate
Increase in the substrate
concentration gradually increases the velocity of enzyme reaction within the limited range of substrate levels. Order of reaction
• When the velocity of the reaction is almost proportional to the
substrate concentration (i.e. [S] is less than Km), the rate of the reaction is said to be first order with respect to substrate.
• When the [S] is much greater than Km, the rate of reaction is independent of substrate concentration, and the reaction is said to be zero order. Enzyme kinetics and Km value • The enzyme (E) and substrate (S) combine with each other to form an unstable enzyme-substrate complex (ES) for the formation of product (P).
• Here k1, k2 and k3 represent the velocity constants for the respective reactions, as indicated by arrows. • Km, the Michaelis-Menten constant, is given by the formula The following equation is obtained after suitable algebraic manipulation • Km or the Michaelis-Menten constant is defined as the substrate concentration (expressed in moles/l) to produce half-maximum velocity in an enzyme catalysed reaction.
• It indicates that half of the enzyme molecules (i.e. 50%) are bound with the substrate molecules when the substrate concentration equals the Km value.
• It is a representative for measuring the strength of ES complex. A low Km
value indicates a strong affinity between enzyme and substrate, whereas a high Km value reflects a weak affinity between them. Lineweaver-Burk double reciprocal plot 3. Effect of temperature
• Velocity of an enzyme reaction
increases with increase in temperature up to a maximum and then declines. A bell-shaped curve is usually observed • The optimum temperature for most of the enzymes is between 35°C–40°C.
• However, a few enzymes (e.g. Taq DNA polymerase, muscle adenylate kinase) are active even at 100°C.
• Some plant enzymes like urease have optimum activity around 60°C. This may be due to very stable structure and conformation of these enzymes.
• In general, when the enzymes are exposed to a temperature above 50°C,
denaturation leading to derangement in the native (tertiary) structure of the protein and active site are seen. Majority of the enzymes become inactive at higher temperature (above 70°C). 4. Effect of pH
Increase in the hydrogen ion
concentration (pH) considerably influences the enzyme activity and a bell-shaped curve is normally obtained • Each enzyme has an optimum pH at which the velocity is maximum.
• Below and above this pH, the enzyme activity is much lower and at extreme pH, the enzyme becomes totally inactive.
• Most of the enzymes of higher organisms show optimum activity around
neutral pH (6–8).
• There are, however, many exceptions like pepsin (1–2), acid phosphatase (4–5) and alkaline phosphatase (10–11).
• Enzymes from fungi and plants are most active in acidic pH (4–6). 5. Effect of product concentration • The accumulation of reaction products generally decreases the enzyme velocity.
• For certain enzymes, the products combine with the active site of enzyme and form a loose complex and, thus, inhibit the enzyme activity. 6. Effect of activators
• Some of the enzymes require certain inorganic metallic cations like
Mg2+, Mn2+, Zn2+, Ca2+, Co2+, Cu2+, Na+, K+ etc. for their optimum activity.
• Metals function as activators of enzyme velocity through various
mechanisms combining with the substrate, formation of ES-metal complex, direct participation in the reaction and bringing a conformational change in the enzyme. 7. Effect of time
• Under ideal and optimal conditions (like pH, temperature etc.), the time required for an enzyme reaction is less.
• Variations in the time of the reaction are generally related to the
alterations in pH and temperature. 8. Effect of light and radiation
• Exposure of enzymes to ultraviolet, beta, gamma and X-rays
inactivates certain enzymes due to the formation of peroxides. e.g. UV rays inhibit salivary amylase activity.
