Luciferase.
The enzyme has an optimal point of pH at which the enzyme works best. For example a catalase enzyme works best in a pH of 7. When the pH changes it denatures the enzyme causing it to not be able to react with the substrate.
enzyme works as a catalyst before and after the reaction it is preserved
55 CThis enzyme works best at a temperature of 50 C and a pH of 12.If the enzyme will be above this temperature, it will denature.
The enzyme with lowest pH optimum is pepsin. Pepsin works in the stomach in an acidic environment and aids in digestion.
Every enzyme works at its maximum rate at a specific temprature called as optimum temprature for that enzyme. AND all enzymes work at their maximum rate at narrow range of pH, called as optimum pH. A slight increase or decrease in pH causes the retardation in enzyme activity or blocks it completely.
Bioluminescence generally works because of bacteria dwelling within the animal's body. For example, an anglerfish's lure is bioluminescent because of a specie of bacteria residing there and taking their nutrition from the anglerfish.
The shape allows the enzyme to carry out specific chemical reactions.
The substrate is the molecule(s) that an enzyme works on
main memory
Substrate
These are either a vitamin or mineral that works with an enzyme. The enzyme doesn't work without it (them).
true
enzyme works as a catalyst before and after the reaction it is preserved
The enzyme has an optimal point of pH at which the enzyme works best. For example a catalase enzyme works best in a pH of 7. When the pH changes it denatures the enzyme causing it to not be able to react with the substrate.
lipase
It depends on the enzyme that you want to test. If the enzyme uses or produces a compound that is detectable, and you know what compounds the enzyme needs to use/produce this, you can add a known amount of the substrate (the compound that is used) to the enzyme and measure the product (the compound that is produced) over time.Answers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comThis approach only works if there is only one enzyme that can act on the compound you are measuring.If you already have that enzyme in pure form you can make an antibody against it and do an Enzyme linked immunosorbent assay (ELISA) or a Western blot, which will give you a signal if the enzyme is present.
its called a substrate