Enzyme kinetics plotting: Which plot is most commonly used in practice to estimate Vmax from experimental initial-rate data?

Introduction:
Linear transformations of the Michaelis–Menten equation help estimate kinetic parameters like Vmax and Km. This question tests recognition of the most commonly taught plot for extracting Vmax in basic biochemistry labs and exam settings.

Given Data / Assumptions:

• Initial-rate measurements v at various substrate concentrations [S].
• Michaelis–Menten framework holds.
• Goal: estimate Vmax (and optionally Km) from a linear graph.

Concept / Approach:
The Lineweaver–Burk plot (double-reciprocal, 1/v versus 1/[S]) linearizes v = (Vmax * [S]) / (Km + [S]) so that the y-intercept equals 1/Vmax and the x-intercept equals −1/Km. It is historically the most “commonly used” and widely taught method despite known weighting issues at low [S].

Step-by-Step Solution:
Write 1/v = (Km/Vmax) * (1/[S]) + 1/Vmax.Plot 1/v (y-axis) against 1/[S] (x-axis).Determine Vmax from the y-intercept: y-intercept = 1/Vmax so Vmax = 1/(y-intercept).Optionally compute Km from the x-intercept: x-intercept = −1/Km.

Verification / Alternative check:
The Eadie–Hofstee (v versus v/[S]) and Hanes–Woolf ([S]/v versus [S]) transformations also allow Vmax estimation, but Lineweaver–Burk remains the classical teaching standard.

Why Other Options Are Wrong:
Langmuir plot: more associated with adsorption isotherms; not standard for enzyme classes in most curricula.
Eadie–Hofstee plot: valid and useful, but the prompt asks for the most commonly used/known method, which is Lineweaver–Burk.
All of these: not correct because Langmuir is not the conventional enzyme-kinetics choice for Vmax estimation in basic courses.

Common Pitfalls:

• Over-relying on points at very low [S], which can distort Lineweaver–Burk lines.
• Confusing x- and y-intercepts when extracting parameters.

Final Answer:
Lineweaver–Burk plot