Enzyme kinetics

Sodium taurocholate. In the absence of the pure sodium taurocholate, the activity in the range of pH 4.0-4.8 was considerably lower. However, in the presence of pure Sodium taurocholate, leukocyte GCase was optimally active at pH 5.0, after which the enzyme activity started to decline. Figure 1 also shows that leukocyte glucocerebrosidase activity is completely dependent upon this detergent. Maximum stimulation representing a four- to five-fold increase in activity occurred…

Introduction An enzyme is a protein that functions as a catalyst, it speeds up chemical reactions (Freeman et al. 2017 p. 90). Enzymes are often large globular proteins and are able to hold substrates in specific orientations so they are able to react, the location where the substrate binds with the enzyme and reacts is called the active site and is the location where the catalysis occurs (Freeman et al. 2017). Enzymes activity is often related to the optimal environment for them in respect to…

it will result in faster rates of enzyme activity. Therefore, if the opposite were to occur, then the reaction will slow down and not function properly. For concentration, my hypothesis was proved to be correct. The undiluted solution had higher frequencies of collision at the active site of the enzyme and substrate. Which means the percent of amylose as well as absorbance level was higher compared to the diluted samples. The result on the effect of pH on enzyme activity prove my hypothesis to…

and the amount of energy available for the reaction. The reaction rate of any enzymes, including α-Amylase, is directly proportional to the temperature before it reaches a certain limit. As the temperature reaches this limit (which was observed to be 37°C in this experiment) , causing the reaction to also be the speed up the most, it is high enough to denature the protein composition of the enzyme, resulting in the enzyme losing its initial shape and therefore the ability to bind securely to a…

other enzymes studied were more effective for anthraquinone-dye (Reactive Blue19) than azo-dye…

modification of the substrate $S_0$ to $S_1$, with enzyme $E$ and phosphatase $F_1$. $S_1$ acts as an enzyme for the modification of the substrate $P_1$ to $P_2$, and this has a phosphatase $F_2$. The following matrices describe the system, The method draws the conclusion that the family is $S$-injective, using the determinant criterion, in the first iteration Consider the modification of the substrate $S_0$ to $S_1$, with enzyme $E$. $S_1$ acts as an enzyme for the modification of the…

reaction without being consumed in the process4. Enzymes are proteins that act as catalysts to a given biochemical reaction4. Enzymes manage to expedite metabolic reactions by lowering the activation energy required for the reaction to proceed4. In ideal conditions, the reactant macromolecule binds and acts on what is referred to as a substrate. However, enzymes require specific conditions specific conditions to perform most effectively4. Enzymes are susceptible to altering their optimal form…

to denature the protein even at a low concentration. There were few sources of errors during the experiment. During experiment 1, the enzymes were kept in the heating block for little too long. Heat exposed to the protein hardens the enzyme, and thus, makes it harder and longer for substrate to bind to it. In experiment 4, with pH value of 9, the TEM-1 enzyme and nitrocefin did react, however, the colour was so faint that it was seen, and therefore, was not recorded. Observing just the…

After reading R.J. Francois' journal, titled "Growth Kinetics of Hydroxide Flocs," it became clear how the number of particles, molecules, or atoms present in the reactants makes it more likely for a reaction to occur at a faster rate. In this study, Francois developed a procedure involving volume concentration…

Introduction Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is the key enzyme for carbon fixation and four different holoenzyme form of Rubisco are found in different organisms (Tabita et al., 1999; Tabita et al., 2007). Most abundant Rubisco forms 1 consist of eight large subunits and eight small subunits are found in algae, cyanobacteria and higher plants (Shively et al., 1973). The multiple nuclear gene encoding small subunits of Rubisco is called rbcS. rbcS exists only in Rubisco…