Enzyme kinetics in industrial applications

Principles of enzyme kinetics have been reviewed in textbooks by Marangoni (2003) and Comish-Bowden (2004). The rate of any chanical reaction follows strict mathematical rules, and understanding of the rules is important for correct predictions of the process timing, particularly in industrial scale processing. The following section briefly introduces some basic aspects of the enzyme kinetics with particular focus on lipases. 

Enzyme (E) accelerates conversion between a substrate (S) and a product (P) by formation of the intermediate binding complexes ES and EP. 

Initially, the reaction proceeds forward in the absence of product. The rate of the reaction at this stage (v=v ) depends only on the substrate concentration and follows the Michaelis-Menten equation. 

The most common biochemical reactions typically involve two substrates (A and B) and one or two product (P and Q)  

The initial reaction rate (v=v at p, q=0) obeys the general equation below with two variables  

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