The optimum temperature of different amylase reactions is different. The optimum temperature of salivary amylase and pancreatic amylase is 37℃, while the optimum temperature of industrial bacteria α -amylase is 60℃.
The blue reaction between starch and iodine is the most sensitive in weak acidic environment with pH=3~5.
Extended data:
Enzyme is inhibited by macromolecular inhibitors or small molecular substances, thus affecting its activity. For example, a macromolecular trypsin inhibitor can inhibit the activity of trypsin. The activity of small molecular inhibitors such as some reaction products, such as 1, 3- diphosphoglycerin mutase, is inhibited by its product, 2,3-diphosphoglyceric acid, so this reaction can be regulated.
In addition, some inorganic ions can inhibit some enzymes and activate others, thus regulating their activities. The activity of enzyme can also be regulated by macromolecular substances, for example, anti-hemophilia factor can enhance the activity of serine protease, so it can obviously promote the coagulation process.
Determine the time required to complete a certain amount of reaction, such as the activity determination of α-amylase. Because iodine has a blue reaction to starch, when amylase is added to starch solution, the blue reaction of iodine disappears and appears red-brown; The disappearance time of iodine reaction to starch color can indicate the activity of amylase. The shorter the reaction time of iodine to the disappearance of starch color, the higher the enzyme activity.