CBSE Class 12-science Answered
1) In competitive inhibition, the Vmax does not change because increasing amounts of substrate can swamp the inhibitor (present in fixed concentration), allowing the enzyme to effectively not see the inhibitor at high substrate concentrations.
On the other hand, the apparent Km for competitive inhibition goes up because it takes more substrate to get the competitively inhibited reaction to Vmax/2.
2) In non-competitive inhibition, the Km does not change. This is because Km is a measure of the affinity of the enzyme for its substrate and this can only be measured by active enzyme.
The fixed amount of inactive enzyme in non-competitive inhibition does not affect the Km and the Km, therefore is unchanged.