The Effect Of Enzymes On The Enzymes

Enzymes are types of proteins that work as a substance to help speed up a chemical reaction (Madar & Windelspecht, 104). There are three factors that help enzyme activity increase in speed. The three factors that speed up the activity of enzymes are concentration, an increase in temperature, and a preferred pH environment. Whether or not the reaction continues to move forward is not up to the enzyme, instead the reaction is dependent on a reaction’s free energy. These enzymatic reactions have reactants referred to as substrates. Enzymes do much more than create substrates; enzymes actually work with the substrate in a reaction (Madar &Windelspecht, 106). For reactions in a cell it is

Enzymes are very large globular proteins with three dimensional shapes which is vital for enzyme activity as natural catalyst in chemical reactions within the living organisms (7).

All enzymes are structured to react with unique substrates. and each enzyme has an active site where the substrate bonds to the enzyme. The active site of an enzyme is shaped to fit the specific substrate it reacts with.

Using the yellow tube, which included everything but starch, as the blank, each group zeroed their spectrophotometer. This was done so that any absorbance observed depends only on the amount of starch present, not on any other reagents (buffer, IKI). To zero the spectrophotometer, the wavelength was first set at 580nm, using knob 3 (45). Next, the groups made sure that the light next to “transmittance” was lit, and the chamber to be tightly closed. Having the chamber empty & closed tightly provides reference for the darkest condition possible. Using knob 1, the transmittance was turned until it read 0.0 (45). Before the groups used their blank test tube to zero the spectrophotometer, each needed to wipe the tube with kimwipes to ensure a clean reading. Turning knob 2, each group was then instructed to zero the absorbance, 0.000. Upon removing the blank, each trial was inserted into the chamber (46). The

Substrate concentration also affects the rate of reaction as the greater the substrate concentration the faster the rate of reaction and all the active sites are filled. At this point the rate of reaction can only be increased if you add more enzymes in to make more active sites available.

In this experiment we tested the effects that enzymes and substrate have on chemical reaction rates, which is the rate at which chemical reactions occur.. This experiment tested how different concentrations of enzyme and substrate affected the light absorption measurements on a spectrophotometer. The experiment also tested how temperature affected the light absorption, and in a separate test, the effect of the enzyme inhibitor hydroxylamine was also tested. In the first test conducted, 3 different concentrations of enzyme, and three different concentrations of substrate were measured in a spectrophotometer. For the enzyme and the substrate, the measurements got higher as the concentrations were higher, but the over measurements of the substrate were smaller than those of the enzyme. In the second test conducted, the medium concentration enzyme was tested under the temperatures; 4°C, 23°C, 37°C, and 60°C. The measurements in this test got higher as the temperature got higher, but did the measurements under 4°C were overall significantly higher than the other temperature measurements. Lastly, the last test conducted showed that the measurements of the substance with 0 and 1 drop of hydroxylamine inhibitor went up, but the measurements of the enzyme with 5 drops of hydroxylamine inhibitor stayed rather low and did not change much. In conclusion, these experiments showed that chemical reaction rates are sped up with higher concentrations of enzyme, substrate,

Enzymes need substates in order to have a reaction and be able to form a enzyme-substrate complex. To summarize this you need "Enzyme+Substrate ->Enzyme-Substrate Complex ->Enzyme+Product". In order for this to happen the Enzyme needs a active site, it's where the enzyme and substrate can bond to each other and are able to

After the substrate solution was added, five drops of the enzyme were quickly placed in tubes 3, 4 and 5. There were no drops of enzyme added in tubes 1 and 2 and in tube 6 ten drops were added. Once the enzyme solution has been added the tubes were then left to incubate for ten minutes and after five drops of DNSA solution were added to tubes 1 to 6. The tubes were then placed in a hot block at 80-90oC for five minutes. They were then taken out after the five minute period and using a 5 ml pipette, 5 ml of distilled water were added to the 6 tubes and mixed by inversion. Once everything was complete the 6 tubes were then taken to the Milton Roy Company Spectronic 21 and the absorbance of each tube was tested.

Most enzymes have pockets on their surface called active sites.

“Enzymes are proteins that have catalytic functions” [1], “that speed up or slow down reactions”[2], “indispensable to maintenance and activity of life”[1]. They are each very specific, and will only work when a particular substrate fits in their active site. An active site is “a region on the surface of an enzyme where the substrate binds, and where the reaction occurs”[2].

1b. Enzymes are proteins that act as biological catalysts. A catalyst is something that speeds up a reaction without changing its form. Enzymes speed up reactions by lowering the activation energy of a reaction. The activation energy of a

Enzymes are organic catalysts that speed up chemical reactions within the body. Enzymes are specific for one particular reaction or group of related reactions. Enzymes are large globular protein molecules with one or more indentations on their surface called active sites, an active site is the part of the enzyme that binds to the substrate, the active site has a specific shape that will bind to a specific substrate. For an enzyme to catalyse a reaction the small substrate molecules must temporarily bind to the active sites of the enzymes were the bonds in the substrate are broken and the products released.

Introduction: Enzymes are specifically folded proteins which catalyse biological reactions in living organisms, they consist of an active site in which specific substrates can enter and a reaction takes place. As the enzyme does not permanently change structure, meaning the active site stays the same it allows multiple substrates to complete the reaction through single enzymes. The substrates are complementary to the active site of the enzyme and can be synthesised or degraded in order to create new products useful to the organism. Enzymes enable the substrates to be orientated in a way that allows for the reaction to take place more readily without relying on the chance of accurately positioned collisions of particles with sufficient energy.

Enzymes are natural catalysts that work from the ability to increase the rate of reaction by decreasing the activation energy of a reaction. (Blanco, Blanco 2017) An enzyme can do this 10^8- to 10^10 fold, sometimes even 10^15 fold. (Malacinsk, Freifelder 1998) The substrate will momentarily bind with the enzyme making the enzyme-substrate complex, of which the shape of the substrate is complimentary to the shape of the active site on the enzyme it is binding with. There are two main theories as to how an enzymes and substrates interact, the lock-and-key model and induced fit theory. The lock-and-key model suggests that the enzyme has a specific shape that fits the substrate and only that substrate. The induced fit theory says the active site and substrate are able to change shape or distort for the reaction to take place with (Cooper,

Enzymes are proteins that act as catalysts and help reactions take place. In short, enzymes reduce the energy needed for a reaction to take place, permitting a reaction to take place more easily. Some enzymes are shape specific and reduce the energy for certain reactions. Enzymes have unique folds of the amino acid chain which result in specifically shaped active sites (Frankova Fry 2013). When substrates fit in the active site of an enzyme, then it is able to catalyze the reaction. Enzyme activity is affected by the concentrations of the enzymes and substrate present (Worthington 2010). As the incidence of enzyme increases, the rate of reaction increases. Additionally, as the incidence of substrate increases so does the rate of reaction.