If the enzyme maltase has a Vo of 0.25 mM per minute when [S] = 0.10 mM, and a Vo of 0.40 mM per minute when [S] = 0.40 mM, what is its y-intercept on a Lineweaver-Burk plot? A. 0.10 minutes per mM B. 0.20 minutes per mM C. 0.50 minutes per mM D. 1.0 minutes per mM E. 2.0 minutes per mM

Enzymes kinetics - is the study of the reaction rate of enzyme catalyzed reactions. The reaction rate is measured with effects of varying substrate concentrations and also varying the other conditions like temp, pH, effect of inhibitors and activators.

Michaelis Menten kinetics curve is the representation of Substate concentration V/S reaction rate which is based on Michaelis Menten equation. Non-linearity of Michaelis Menten kinetics curve makes the estimation of Vmax and Km difficult, thus, researched modified the Michaelis Menten equation and developed linear graph in Lineweaver Burk plot for accurate calculation of Km and Vmax. Lineweaver Burk plot is the representation of 1/S Vs 1/Vo, i.e. reciprocal of S and Vo , that is why it is also called as double reciprocal plot. Both plots/curves are used to derived Vmax and Km values.

Vmax is the maximum velocity of chemicals reaction and Km is the substrate concentration at which half of Vmax is achieved. Higher the Km, lower the affinity of enzyme for substate and eventually high substrate concentration required for the reaction to occur.