The effect of enzyme inhibitor concentration on the reaction velocity of alpha-amylase enzyme in starch hydrolysis can be described using enzyme kinetics principles. Enzyme inhibitors are molecules that bind to enzymes and decrease their activity. There are two main types of enzyme inhibitors: competitive and non-competitive inhibitors.1. Competitive inhibitors: These inhibitors compete with the substrate in this case, starch for the active site of the enzyme alpha-amylase . As the concentration of the competitive inhibitor increases, it occupies more active sites of the enzyme, leaving fewer sites available for the substrate to bind. This results in a decrease in reaction velocity. However, the maximum reaction velocity Vmax remains the same, as it can still be reached if the substrate concentration is high enough to outcompete the inhibitor. The apparent affinity of the enzyme for the substrate Km increases, meaning that a higher substrate concentration is needed to achieve half of the maximum reaction velocity.2. Non-competitive inhibitors: These inhibitors bind to a different site on the enzyme, not the active site, and cause a conformational change in the enzyme that reduces its activity. As the concentration of the non-competitive inhibitor increases, the reaction velocity decreases. In this case, the maximum reaction velocity Vmax decreases, as even high substrate concentrations cannot overcome the inhibitory effect. However, the apparent affinity of the enzyme for the substrate Km remains the same, as the substrate can still bind to the enzyme with the same affinity.In summary, as the concentration of an enzyme inhibitor competitive or non-competitive increases, the reaction velocity of alpha-amylase enzyme in starch hydrolysis will decrease. The specific effects on Vmax and Km depend on the type of inhibitor. To counteract the inhibitory effect, increasing the substrate concentration can help in the case of competitive inhibitors, but not for non-competitive inhibitors.