Question

General Biology / Biol 101 REVIEW QUESTIONS ON ENZYME KINETICS 10) Why did we do all of our work in a water bath and use buffer in all of our tubes? 11) What happens to velocity of an enzyme catalyzed reaction as we increase the amount of initial substrate available with a constant amount of enzyme? Be specific. 12) What is the purpose of calculating Km? (What does it tellus about an enzyme?) 13) What are the advantages of the Lineweaver-Burk Plot? Be specific

Answer 1

Solution

Que 10 answer

• we used water bath and buffer solution to enzyme catalyzed reaction because- oftenly the rate of many enzymatic reaction is increases with increase in temperature.
• if we increase temperature by 10 celcius then enzyme activity get increased upto 50 to 100 percent.
• temperature increases the kinetic motion of all molecule in test tube to start more contact of substrate with enzyyme to increase turnover and rate of reaction.
• the buffer are the solution of weak acid and strong base. Which stablizes the pH of environment of enzyme catalysed reaction.
• for each biochemical reaction enzymes shows there maximum activity at certain pH range as well as substrate also do available and interact at specific pH.
• if small change in pH occure in such reaction then it will affects the stability and of enzyme and substrate.so we add buffer in reaction solution.

Que 11 answer

• if we increase the substrate concentration with constant number of enzyme molecules then velosity of reaction increase maximum until all enzyme molecule converted into Enzyme substarte complex.
• initialy not all enzyme molecule are engaged in enzyme substarte complex but if substrate molecule increases gradually ES complex increases. At maximum velosity the rate of reaction will constant though we continously adding substrate because all enzyme molecules are saturated with its substrate.

Que 12 answer

• the aim of calculating Km is to know enzyme has more or less affinity towards substrate.
• the km is the substrate concentration at which reaction attains 1/2 maximum velosity.
• if km is low then it indicate that enzyme has more affinity to its substrate so reaction will attain fast 1/2 Vmax.so small amount of substrate is required to saturate enzyme.
• if km is more then it indicate that enzyme has low affinity towards its substrate so reaction will attain slow 1/2 Vmax.so large amount of substrate is required to saturate anzyme.

Que 13 answer-advantages of Lineweaver burk plot are

• it gives more acurate estimate Vmax and precise acuracy of enzyme inhibition.
• it gives linear idea of km value and maximum velosity.
• it has advantage for to identify compitative, non compitative and uncompitative enzyme inhibition.
• specific enzyme reaction mechanism also can be understood by using this plot.