How does the amount of BAPNA digestion varies with time?

The digestion of BAPNA (Benzoyl-DL-arginine-p-nitroanilide) by trypsin follows typical Michaelis-Menten enzyme kinetics. The rate of digestion increases with time initially as more enzyme molecules become engaged in the reaction. However, as the substrate concentration decreases over time, the rate of digestion slows down. The relationship between the amount of BAPNA digested and time can be described by the following equation:

[BAPNA]t = [BAPNA]0 - k[E][BAPNA]0*t

Where:

- [BAPNA]t: Amount of BAPNA digested at time t

- [BAPNA]0: Initial concentration of BAPNA

- k: Rate constant for the reaction

- [E]: Concentration of trypsin

- t: Time

The plot of [BAPNA]t versus t typically shows a hyperbolic curve. The initial linear phase of the curve represents the period when the reaction rate is constant and proportional to the enzyme concentration. As the reaction progresses, the curve levels off due to substrate depletion and the decreasing rate of digestion.

By measuring the initial velocity (Vo) of the reaction and determining the Michaelis-Menten constant (Km) through graphical analysis (e.g., Lineweaver-Burk or Hanes-Woolf plots), it's possible to characterize the enzyme kinetics and gain insights into the catalytic efficiency and substrate affinity of trypsin for BAPNA.