This chapter is from the book
This chapter is from the book
This chapter is from the book
3.6. Summary
Enzymes are protein or glycoprotein molecules that catalyze biologically important reactions. Some RNA molecules may have catalytic activity too. Enzymes are very effective, specific, and versatile biocatalysts. Enzymes bind substrate molecules and reduce the activation energy of the reaction catalyzed, resulting in significant increases in reaction rate. Some protein enzymes require a nonprotein group for their activity as a cofactor.
Simple single-enzyme–catalyzed reaction kinetics can be described by Michaelis–Menten kinetics, which has a hyperbolic form in terms of substrate concentration. The activity of some enzymes can be altered by inhibitory compounds, which bind the enzyme molecule and reduce its activity. Enzyme inhibition may be competitive, noncompetitive, and uncompetitive. High substrate and product concentrations may be inhibitory, too. Enzyme activators increase enzymatic reaction rate upon binding the enzyme molecules.
Enzymes require optimal conditions (pH, temperature, ionic strength) for their maximum activity. Enzymes with an ionizing group on their active site show a distinct optimal pH that corresponds to the natural active form of the enzyme. The activation energy of enzyme–catalyzed reactions is within 4 to 20 kcal/g-mol. Above the optimal temperature, enzymes lose their activity, and the inactivation energy is on the order of 40 to 130 kcal/g-mol.
Enzymes can be used in suspension or in immobilized form. Enzymes can be immobilized by entrapment in a porous matrix, by encapsulation in a semipermeable membrane capsule or between membranes, such as in a hollow-fiber unit, or by adsorption onto a solid support surface. Enzyme immobilization provides enzyme reutilization, eliminates costly enzyme recovery and purification processes, and may result in increased activity by providing a more suitable microenvironment for the enzyme. Enzyme immobilization may result in diffusion limitations within the matrix. Immobilization may also cause enzyme instability, loss of activity, and a shift in optimal conditions (pH, ionic strength). To obtain maximum reaction rates, the particle size of the support material and enzyme loading need to be optimized, and a support material with the correct surface characteristics must be selected.
Enzymes are widely used in industry and have significant medical applications. Among the most widely used enzymes are proteases (papain, trypsin, subtilisin), amylases (starch hydrolysis), rennet (cheese manufacturing), glucose isomerase (glucose-to-fructose conversion), glucose oxidase (glucose-to-gluconic acid conversion), lipases (lipid hydrolysis), and pectinases (pectin hydrolysis). Enzyme production and utilization are a multibillion-dollar business with a great potential for expansion.