Lasto B. answered 10/08/19
Experienced Medical Biochemistry - "Soon to be" M.D.
Hope you find this helpful:
Enzymes are catalysts, but the major property is that they are proteins. So the structure of the tertiary protein such as an enzyme has different bonds that hold it to maintain its conformation (structural shape and size). These bonds can be classified as covalent and noncovalent bonds. The covalent bonds are the bonds between atoms that make up the primary structure where's the noncovalent are basically more like interactions between primary structures, which then form or fold into secondary, then tertiary and quaternary structures.
With that being said, we now understand that there are different factors that may affect the structure of an enzyme. These are mainly 3: 1) Temperature, 2) pH, and 3) substrate. I will focus on temperature since its your inquiry, kindly message me for more.
Increase in temperature will increase the kinetic energy of particles in a substance. Kinetic energy (kE) is energy possessed in motion. So increase in kE will increase the movement of particles, which cause the randomness. The degree of randomness of particles in a substance is what we call entropy. Therefore, increase in temperature, increase kE which increase entropy. So, if temperature is increase the randomness thus also increasing the heat energy. heat energy will increase conformational flexing (size and shape changes) of the enzyme. If the temperature is increased beyond optimum level then the noncovalent bonds/interactions will be disrupted and enzyme protein structure will be unfolded. The process of unfolding is called denaturation, so they are denatured. If the confirmation is changed then therefore the active site is disrupted and so the substrate can not attach to enzyme active site. Therefore no enzyme reaction will occur. Bottomline: increase in temperature, increases enzyme activity unlike optimum level (45-55C) is reached. Beyond optimum rate of reaction will fall.
Message me for more question and clarifications. Thank you. happy studying.