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Importance of enzymes in biology
Enzymes and their importance
Reactions using enzymes
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All biological processes require a constant supply of energy. The fabrication and regulation of energy is a result of catalytic reactions that occur in cells by enzymes. Enzymes typically contain a few active sites that enable substrates (reactants) to bind to their designated enzyme and form an enzyme-substrate complex, to then release the product (Alberte J. , Pitzer T. , Calero K.). In order for an enzyme to release a product, the reactant molecules must absorb enough energy from their surroundings to reach the unstable transition state and form new bonds at a faster rate without the denaturization of the enzyme. Enzymes have sets of conditions at which they are enabled to work properly, known as the optimal condition. For experiment 4,
In this experiment the enzyme peroxidase and the substrate hydrogen peroxide were not mixed initially, instead they were both placed in separate tubes and were incubated at a specific temperature, to prevent hydrogen peroxide from undergoing any reaction with peroxidase until they both acquire the required temperature.
Living organisms undergo chemical reactions with the help of unique proteins known as enzymes. Enzymes significantly assist in these processes by accelerating the rate of reaction in order to maintain life in the organism. Without enzymes, an organism would not be able to survive as long, because its chemical reactions would be too slow to prolong life. The properties and functions of enzymes during chemical reactions can help analyze the activity of the specific enzyme catalase, which can be found in bovine liver and yeast. Our hypothesis regarding enzyme activity is that the aspects of biology and environmental factors contribute to the different enzyme activities between bovine liver and yeast.
One of the most primitive actions known is the consumption of lactose, (milk), from the mother after birth. Mammals have an innate predisposition towards this consumption, as it is their main source of energy. Most mammals lose the ability to digest lactose shortly after their birth. The ability to digest lactose is determined by the presence of an enzyme called lactase, which is found in the lining of the small intestine. An enzyme is a small molecule or group of molecules that act as a catalyst (catalyst being defined as a molecule that binds to the original reactant and lowers the amount of energy needed to break apart the original molecule to obtain energy) in breaking apart the lactose molecule. In mammals, the lactase enzyme is present
The affects of pH, temperature, and salt concentration on the enzyme lactase were all expected to have an effect on enzymatic activity, compared to an untreated 25oC control. The reactions incubated at 37oC were hypothesized to increase the enzymatic activity, because it is normal human body temperature. This hypothesis was supported by the results. The reaction incubated to 60oC was expected to decrease the enzymatic activity, because it is much higher than normal body temperature, however this hypothesis was not supported. When incubated to 0oC, the reaction rate was hypothesized to decrease, and according to the results the hypothesis was supported. Both in low and high pH, the reaction rate was hypothesized to decrease, which was also supported by the results. Lastly, the reaction rate was hypothesized to decrease in a higher salt concentration, which was also supported by the results.
Mader, S. S. (2010). Metabolism: Energy and Enzymes. In K. G. Lyle-Ippolito, & A. T. Storfer (Ed.), Inquiry into life (13th ed., pp. 105-107). Princeton, N.J: McGraw Hill.
Enzymes are biological catalysts, which are proteins that help speed up chemical reactions. Enzymes use reactants, known as the substrates, and are converted into products. Through this chemical reaction, the enzyme itself is not consumed and can be used over and over again for future chemical reactions, but with the same substrate and product formed. Enzymes usually only convert specific substrates into products. Substrates bind to the region of an enzyme called the active site to form the enzyme/substrate complex. Then this becomes the enzyme/products complex, and then the products leave the enzyme. The activity of enzymes can be altered based on a couple of factors. Factors include pH, temperature and others. These factors, if they become
This hurdle is called the activation energy of the reaction. [IMAGE] By decreasing the activation energy, more substrate is changed to product in a certain amount of time. That is, the enzyme increases the rate of the reaction. [IMAGE] The activity of catalase can be measured by finding the rate of which the oxygen gas is released from the breakdown of Hydrogen Peroxide.
Jim Clark. (2007). The effect of changing conditions in enzyme catalysis. Retrieved on March 6, 2001, from http://www.chemguide.co.uk/organicprops/aminoacids/enzymes2.html
The purpose of the study is to identify an unknown microorganism using multiple microbiology lab techniques. Through this process I will gain knowledge on how to perform these techniques as well as the importance of these tests on identifying unknown microorganisms. This is significant as the goal of this course is to familiarize ourselves with the common microbiology tests as well as the microorganisms we encounter in our daily activities.
According to the graph on amylase activity at various enzyme concentration (graph 1), the increase of enzyme dilution results in a slower decrease of amylose percentage. Looking at the graph, the amylose percentage decreases at a fast rate with the undiluted enzyme. However, the enzyme dilution with a concentration of 1:3 decreased at a slow rate over time. Additionally, the higher the enzyme dilution, the higher the amylose percentage. For example, in the graph it can be seen that the enzyme dilution with a 1:9 concentration increased over time. However, there is a drastic increase after four minutes, but this is most likely a result of the error that was encountered during the experiment. The undiluted enzyme and the enzyme dilution had a low amylose percentage because there was high enzyme activity. Also, there was an increase in amylose percentage with the enzyme dilution with a 1: 9 concentrations because there was low enzyme activity.
The [ES] complex can then undergo two different pathways; the complex can dissociate to [E] and [S], at a rate of k or it can shift equilibrium to the left with a rate constant of k2 to form [E] and product [P]1. In this model, the breakdown of the ES complex to yield P is the overall rate-limiting step. Three assumptions of a Michaelis-Menton plot are that a specific [ES] complex in rapid equilibrium between [E] and [S] is a necessary intermediate, the amount of substrate is more than the amount of enzyme so the [S] remains constant, and that this plot follows steady state assumptions. Steady state assumptions states that the intermediate stays the same concentration even if the starting materials and products are constantly changing.2 The rapid equilibrium between enzyme and substrate, and the enzyme-substrate complex yields a mathematical description regarded as the Michaelis-Menton
This line graph shows how some phenotypes were more successful than others. This is an accurate representation of natural selection. The dark blue, pink, and orange phenotypes became extinct before the experiment was even finished. The successful phenotypes were green, purple, and yellow.
Materials used in the experiment included 5-7 g of the potato tissue, 50ml of 2.0M phosphate buffer coffee filter and guaiacol dye.
Enzymes work by lowering the activation energy required by molecules to start the reaction off. Enzymes also react (reversibly) with substrates (The molecule(s) that the enzyme is catalysing) this is done by forming Enzyme-substrate complex, which is then broken down into products. As well as being affected by temperature and pH enzymes optimum rate of reaction is also changed by competitive and non competitive inhibitors. Competitive inhibitors inhibit the enzyme so that enzyme-substrate complex’s cant form until it’s unblocked or there is a change in concentration in substrate, this means it takes longer to reach the optimum rate of reaction.
In this lab, it was determined how the rate of an enzyme-catalyzed reaction is affected by physical factors such as enzyme concentration, temperature, and substrate concentration affect. The question of what factors influence enzyme activity can be answered by the results of peroxidase activity and its relation to temperature and whether or not hydroxylamine causes a reaction change with enzyme activity. An enzyme is a protein produced by a living organism that serves as a biological catalyst. A catalyst is a substance that speeds up the rate of a chemical reaction and does so by lowering the activation energy of a reaction. With that energy reactants are brought together so that products can be formed.