Agro-industrial waste impacts populations worldwide. Food waste, in turn, is a major source of complex lipids, carbohydrates, and other substances. Therefore, it is crucial to convert food waste into products that reduce environmental problems. Enzymatic hydrolysis has advantages over chemical hydrolysis. Examples include the enzymatic hydrolysis of starch by α-amylase and the hydrolysis of inulin by inulinase, which occur under milder environmental and temperature conditions than acid hydrolysis of starch or inulin. Despite these milder temperature conditions, during substate hydrolysis, enzyme deactivation occurs under exposure to temperature. As temperature increases above Topt (which maximizes catalytic activity), enzyme deactivation becomes more pronounced, leading to a decrease in enzyme activity. Therefore, determining the rate constant of deactivation kd, during biotransformation is an important aspect in understanding enzyme kinetics. Most experimental studies focus on changes in enzyme activity with time and temperature. However, enzyme deactivation also occurs during enzymatic reactions conducted at different temperatures, and this process is characterized by specific deactivation parameters. The study is to present the rate constants of deactivation kd, for selected biotransformation processes. The selected biotransformation processes are hydrolysis of olive oil by lipase, hydrolysis of inulin by inulinase, and hydrolysis of starch by α-amylase. Given the widespread use of enzymes in industry, the information on enzyme deactivation presented in this study can be used by engineers involved in modeling and optimizing enzymatic processes. This knowledge is also essential for the effective and sustainable use of enzymes in industrial applications. It is important to emphasize that the deactivation parameters discussed in this study also carry significant economic, social, and environmental implications.
Miłek et al. (Fri,) studied this question.