The activity of protease inhibitors is influenced by various conditions, which may lead to their loss of activity. Here are several possible scenarios:
High temperature conditions: High temperature can cause denaturation of protease inhibitors, leading to their loss of activity. For example, some protease inhibitors will rapidly inactivate at high temperatures.
Inappropriate pH value: Each enzyme only exhibits high activity within a specific pH range. If the pH value is too high or too low, the enzyme will be irreversibly damaged, with decreased stability, activity, and even inactivation. The appropriate pH range for different enzymes varies, with some being slightly acidic, neutral, or alkaline.
Inhibitory effect: Some substances can weaken, inhibit, or even destroy the action of enzymes, and these substances are called enzyme inhibitors. For example, heavy metal ions (Fe3+, Cu2+, Hg+, Pb+, etc.), carbon monoxide, hydrogen sulfide, organic cations, ethylenediamine, and tetraacetic acid.
Preservation environment: Enzyme preparations are in a dormant state in a low-temperature environment. To ensure long-term preservation of the enzyme without losing its activity, the key lies in a dry and low-temperature environment.
In addition, for some specific protease inhibitors, such as trypsin inhibitors in soybean milk, their inactivation mainly includes two reasons: thiol exchange reaction and thiol oxidation reaction, as well as protein aggregation. Among them, Kunitz type trypsin inhibitors have low thermal stability and are easily inactivated under heating conditions, while Bowman Birk type trypsin inhibitors have high thermal stability and are not easily inactivated.
In summary, the activity of protease inhibitors is influenced by various factors, and corresponding measures need to be taken according to specific circumstances to maintain their activity.
