Biocatalysis Fundamentals: Enzyme Kinetics and Inhibition

Biocatalysis is at the heart of modern green chemistry, biotechnology, and pharmaceuticals, offering highly selective and sustainable chemical pathways. Understanding how enzymes function—and how their activity is regulated or disrupted—is essential for anyone looking to design efficient biochemical reactors and industrial processes. This text-only course provides a clear, step-by-step pathway from basic biochemistry to the quantitative modeling of enzymatic reactions. You will transition from basic concepts to analyzing complex kinetic systems, learning how to mathematically describe and manipulate biocatalytic reactions. What you'll learn: - Understand the fundamental principles of biocatalysis and enzyme-substrate interactions. - Analyze Michaelis-Menten kinetics and interpret key kinetic parameters. - Differentiate between competitive, uncompetitive, and noncompetitive inhibition pathways. - Evaluate the chemical mechanisms behind enzyme toxicity and irreversible inactivation. - Apply kinetic models to practical chemical engineering and modern green chemistry scenarios. The course begins with foundational terminology and the molecular basis of catalysis, then progresses through detailed explanations of reaction rates, inhibition types, and mathematical modeling techniques. Designed for beginners in chemical engineering, bioengineering, or applied chemistry, this course requires no prior background in kinetics. Start reading today to build a strong foundation in biocatalytic design.