because the amount of the other variables are the same, no change. once 4.0 g of lactose substrate or whatever it is is at it's maximum reaction rate, it can do no one reaction therefore there was no reaction in the 8.0 g of substrate.
Because the reaction volume was also doubled; so there was no change in concentration of substrate.
Add more reactants.
Depends on how much substrate the enzyme can process. Most enzymes can process more than one molecule of substrate without denaturing or becoming unusable. However, in the terms of your question. More substrate is better. Too many enzymes would mean the reaction would be cut short, because they would all react the substrate at once. So for a prolonged, efficient reaction more substrate would be proper.
zff
The molecule upon which an enzyme acts is called the substrate.
An enzyme increases the rate of the reaction by lowering the activation energy needed for the reaction. The secret is that enzymes weaken the bonds in the substrate so that products are formed much faster. Enzymes are catalysts or substances that speed up the reaction (without being consumed in it). An enzyme increases the rate of reaction by lowering the energy of activation or (Ea). Enzymes achieve that by attaching to the substrate in the active site and forming an enzyme substrate complex in which the enzyme disturbs the covalent bond of the substrate. This causes it to enter the transitional state, which is the most energetic and unstable state. The enzyme then breaks apart, and the substrate goes into an exorganic reaction to form the product.
The statement in question is partially true. It is right to think that an increase in reaction temperature will result in an increase in the rate of the reaction since the interacting molecules will have more kinetic energy. However, it is important to remember that enzymes are after all proteinacious structures. They have an optimum temperature at which they function best. The reaction conditions must be optimized to hold the reaction steadily at this optimum temperature. If the temperature is too high, the enzyme denatures (degrades due to excess heating) you suck lol
No, since the reaction reaches a max rate depending on the speed of which the Enzyme bonds to the substrate and the speed at which the enzyme catalyzes the reaction to produce enzyme and product (shown below). E + S --> ES (E - enzyme, S - substrate, P - products) ES --> E + P Thus, if each reaction rate is not equal to each other, the rate of the overall reaction is not only proportional to both the concentration of enzyme and substrate.
The Vmax would be the highest rate, when the enzyme is fully saturated. So as you increase substrate the Vmax will increase to a certain point (Vmax). Beyond that point, no matter how much substrate you add the Vmax will not increase.
Depends on how much substrate the enzyme can process. Most enzymes can process more than one molecule of substrate without denaturing or becoming unusable. However, in the terms of your question. More substrate is better. Too many enzymes would mean the reaction would be cut short, because they would all react the substrate at once. So for a prolonged, efficient reaction more substrate would be proper.
zff
The molecule upon which an enzyme acts is called the substrate.
Dunno. But this is pretty cool. But if i search the question, i obvioudly don't know it, so why would i be given an optionto answer it?
An enzyme increases the rate of the reaction by lowering the activation energy needed for the reaction. The secret is that enzymes weaken the bonds in the substrate so that products are formed much faster. Enzymes are catalysts or substances that speed up the reaction (without being consumed in it). An enzyme increases the rate of reaction by lowering the energy of activation or (Ea). Enzymes achieve that by attaching to the substrate in the active site and forming an enzyme substrate complex in which the enzyme disturbs the covalent bond of the substrate. This causes it to enter the transitional state, which is the most energetic and unstable state. The enzyme then breaks apart, and the substrate goes into an exorganic reaction to form the product.
The substrate would be unable to bond preventing the reaction from being catalyzed.
A substrate is a substance in which an enzyme reacts. The substrate for catalase would be hydrogen peroxide otherwise known as H2O2.
The statement in question is partially true. It is right to think that an increase in reaction temperature will result in an increase in the rate of the reaction since the interacting molecules will have more kinetic energy. However, it is important to remember that enzymes are after all proteinacious structures. They have an optimum temperature at which they function best. The reaction conditions must be optimized to hold the reaction steadily at this optimum temperature. If the temperature is too high, the enzyme denatures (degrades due to excess heating) you suck lol
because the competitive inhibitor stops the regular substrate from joining the enzyme. Its takes its place in the enzyme.
the reaction will stop because the introduced substance that binds to the reaction site will change the shape of the reaction site so that the original substrate will no longer fit