The rate of reaction can be determined by measuring the change in optical rotation of the sample as a function of time if a reactant or product is chiral. This technique is especially useful for kinetic studies of enzyme catalysis involving sugars. For example, the enzyme invertase catalyzes the hydrolysis of sucrose, an optically active sugar. The initial reaction rates as a function of sucrose concentration are as follows:

Sucrose]₀ (M)…………………………..Rate (M s^–1)               

0.029……………………………………………..0.182

0.059……………………………………………..0.266

0.088……………………………………………..0.310

0.117……………………………………………..0.330

0.175……………………………………………..0.372

0.234……………………………………………..0.371

Use these data to determine the Michaelis constant for invertase.