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Enzyme coursework evaluation

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However, there were a few minor flaws. Firstly, due to time constraints, it was quite difficult to perform the experiment at exactly the same time of the day. Also, the experiment was based around the schedule of the test subject so the time the experiment was conducted isn't consistent. Also, to check whether or not the maturity state has influence on the change of vitamin C concentration, the newly bought and old lemon were used. It make sense because at this high temperature the enzyme would already become denatured.

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Enzyme Coursework. Investigation to find the effect of substrate concentration on the rate of an enzyme controlled reaction. Extracts from this document Introduction Investigation to find the effect of substrate concentration on the rate of an enzyme controlled reaction Design Aspect 1: Defining the problem and selecting variables Investigation title: is the rate of an enzyme controlled reaction affected by substrate concentration? Conclusion As a result of this, the concentration of the enzyme present on the pieces of paper is uncertain being soaked for a longer time will allow the piece of paper to absorb more catalase, which would speed up the reaction as there would be more of the enzymes.

The above preview is unformatted text. Found what you're looking for? Here's what a star student thought of this essay 5 star s. Response to the question This Biology IA is outstanding in content and presentation, combining very accurate background information, easy-to-follow procedures listed out, relevant data presented in a coherent manner and insightful discussion and evaluation as well. Read full review. Level of analysis The IA definitely exceeds expectations in several aspects of analysis but also needs more improvement in other aspects.

Quality of writing The whole IA has an excellent presentation. Not the one? Search for your essay title Related International Baccalaureate Biology essays The effect of Pectinase Concentraton on the production of apple juice plot the graph was proven appropriate as the results were satisfactory, because it clearly shows the overall trend that was occurring supporting the hypothesis of an increase in apple juice in relation to Pectinase concentration.

Biology Lab Report-Osmosis A solution which brings about such changes is known as hyper-osmotic solution. To investigate how aerobic exercise affects the heart rate However, there were a few minor flaws. Vitamin C concentration Also, to check whether or not the maturity state has influence on the change of vitamin C concentration, the newly bought and old lemon were used. Experiment-Effect of Temperature on the Action of Amylase Enzyme It make sense because at this high temperature the enzyme would already become denatured.

See more essays. Over , pieces of student written work Annotated by experienced teachers Ideas and feedback to improve your own work. Save Sign up now Want to read the rest? Read more The above preview is unformatted text. In addition, commercially important animal and plant enzymes are often located within only one organ or tissue, so the remaining material is essentially a waste product, disposal of which is required.

Finally, enzymes from plant and animal sources show wide variation in yield, and may only be available at certain times of year, whereas none of these problems are associated with microbial enzymes. Microbial enzymes often have properties that make them more suitable for commercial exploitation. In comparison with enzymes from animal and plant sources, the stability of microbial enzymes is usually high. For example, the high temperature stability of enzymes from thermophilic microorganisms is often useful when the process must operate at high temperatures e.

Microorganisms are also very amenable to genetic modification to produce novel or altered enzymes, using relatively simple methods such as plasmid insertion. The genetic manipulation of animals and plants is technically much more difficult, is more expensive and is still the subject of significant ethical concern, especially in the U. Although many enzymes are retained within the cell, and may be located in specific subcellular compartments, others are released into the surrounding environment.

The majority of enzymes in industrial use are extracellular proteins from either fungal sources e. Aspergillus species or bacterial sources e. Bacillus species. Many other enzymes for non-industrial use are intracellular and are produced in much smaller amounts by the cell. Examples of these include asparaginase, catalase, cholesterol oxidase, glucose oxidase and glucosephosphate dehydrogenase.

Within the cell, enzymes are generally found along with other proteins, nucleic acids, polysaccharides and lipids. The activity of the enzyme in relation to the total protein present i. A variety of methods can be used to remove contaminating material in order to purify the enzyme and increase its specific activity.

Enzymes that are used as diagnostic reagents and in clinical therapeutics are normally prepared to a high degree of purity, because great emphasis is placed on the specificity of the reaction that is being catalysed. Clearly the higher the level of purification, the greater the cost of enzyme production. In the case of many bulk industrial enzymes the degree of purification is less important, and such enzymes may often be sold as very crude preparations of culture broth containing the growth medium, organisms whole or fragmented and enzymes of interest.

However, even when the cheapest bulk enzymes are utilized e. The pH may also be adjusted to optimize enzyme stability. If the enzyme-producing organism is a fungus, this may be removed by centrifugation at low speed. If the enzyme source is bacterial, the bacteria are often flocculated with aluminum sulfate or calcium chloride, which negate the charge on the bacterial membranes, causing them to clump and thus come out of suspension. Extracellular enzymes are found in the liquid component of the pretreatment process.

However, intracellular enzymes require more extensive treatment. The biomass may be concentrated by centrifugation and washed to remove medium components. The cellular component must then be ruptured to release the enzyme content. This can be done using one or more of the following processes:. Separation of enzymes from the resulting solution may then involve a variety of separation processes, which are often employed in a sequential fashion. The first step in an enzyme purification procedure commonly involves separation of the proteins from the non-protein components by a process of salting out.

Proteins remain in aqueous solution because of interactions between the hydrophilic water-loving amino acids and the surrounding water molecules the solvent. If the ionic strength of the solvent is increased by adding an agent such as ammonium sulfate, some of the water molecules will interact with the salt ions, thereby decreasing the number of water molecules available to interact with the protein.

Under such conditions, when protein molecules cannot interact with the solvent, they interact with each other, coagulating and coming out of solution in the form of a precipitate. This precipitate containing the enzyme of interest and other proteins can then be filtered or centrifuged, and separated from the supernatant.

Since different proteins vary in the extent to which they interact with water, it is possible to perform this process using a series of additions of ammonium sulfate, increasing the ionic strength in a stepwise fashion and removing the precipitate at each stage. Thus such fractional precipitation is not only capable of separating protein from non-protein components, but can also enable separation of the enzyme of interest from some of the other protein components.

Subsequently a wide variety of techniques may be used for further purification, and steps involving chromatography are standard practice. Ion-exchange chromatography is often effective during the early stages of the purification process. The protein solution is added to a column containing an insoluble polymer e. Proteins whose net charge is opposite to that of the ion-exchange material will bind to it, whereas all other proteins will pass through the column.

A subsequent change in pH or the introduction of a salt solution will alter the electrostatic forces, allowing the retained protein to be released into solution again. Gel filtration can be utilized in the later stages of a purification protocol to separate molecules on the basis of molecular size.

Columns containing a bed of cross-linked gel particles such as Sephadex are used. These gel particles exclude large protein molecules while allowing the entry of smaller molecules. Separation occurs because the larger protein molecules follow a path down the column between the Sephadex particles occupying a smaller fraction of the column volume. Larger molecules therefore have a shorter elution time and are recovered first from the gel filtration column.

Affinity chromatography procedures can often enable purification protocols to be substantially simplified. Typically, with respect to enzyme purification, a column would be packed with a particulate stationary phase to which a ligand molecule such as a substrate analogue, inhibitor or cofactor of the enzyme of interest would be firmly bound.

As the sample mixture is passed through the column, the enzyme interacts with, and binds, to the immobilised ligand, being retained within the column as all of the other components of the mixture pass through the column unrewarded. Subsequently a solution of the ligand is introduced to the column to release elute and thereby recover the bound enzyme from the column in a highly purified form.

Nowadays numerous alternative affinity chromatography procedures exist that are able to separate enzymes by binding to areas of the molecule away form their active site. Advances in molecular biology enable us to purify recombinant proteins, including enzymes, through affinity tagging. In a typical approach the gene for the enzyme of interest would be modified to code for a further short amino acid sequence at either the N- or C- terminal.

For example, a range of polyhistidine tagging procedures are available to yield protein products with six or more consecutive histidine residues at their N- or C- terminal end. When a mixture containing the tagged protein of interest is subsequently passed through a column containing a nickel-nitrilotriacetic acid Ni-NTA agarose resin, the histidine residues on the recombinant protein bind to the nickel ions attached to the support resin, retaining the protein, whilst other protein and non-protein components pass through the column.

Elution of the bound protein can then be accomplished by adding imidazole to the column, or by reducing the pH to to displace the His-tagged protein from the nickel ions. If more highly purified enzyme products are required, other supplemental options are also available, including various forms of preparative electrophoresis e.

Enzymes are antigenic, and since problems occurred in the late s when manufacturing workers exhibited severe allergic responses after breathing enzyme dusts, procedures have now been implemented to reduce dust formation. Although many industrial processes, such as cheese manufacturing, have traditionally used impure enzyme sources, often from animals or plants, the development of much of modern industrial enzymology has gone hand in hand with the commercial exploitation of microbial enzymes.

These were introduced to the West in around when the Japanese scientist Jokichi Takamine settled in the U. The principal product was Takadiastase, a mixture of amylolytic and proteolytic enzymes prepared by cultivating the fungus Aspergillus oryzae on rice or wheat bran. Takadiastase was marketed successfully in the U.

The enzyme was primarily used within the textile industry for the removal of the starch that protects the warp in the manufacture of cotton. In around it was found that fungal pectinases could be used in the preparation of fruit products.

In subsequent years, several other hydrolases were developed and sold commercially e. After World War Two the fermentation industry underwent rapid development as methods for the production of antibiotics were developed. These methods were soon adapted for the production of enzymes.

In the s, glucoamylase was introduced as a means of hydrolysing starch, replacing acid hydrolysis. Subsequently, in the s and s, proteases were incorporated into detergents and then glucose isomerase was introduced to produce sweetening agents in the form of high-fructose syrups.

Since the s, lipases have been incorporated into washing powders, and a variety of immobilized enzyme processes have been developed see section on enzyme immobilization , many of which utilize intracellular enzymes. Currently, enzymes are used in four distinct fields of commerce and technology Table 6 :.

Around 40—50 enzymes are produced on an industrial scale i. The global enzyme market is currently dominated by the hydrolases, especially the proteases, together with amylases, cellulases and lipases supplied either as liquid concentrates or as powders or granules that release the soluble enzyme on dissolution.

The developing economies of the Asia-Pacific Region, the Middle East and Africa are now seen to be emerging as the fastest growing markets for industrial enzymes. Microbial enzymes are typically produced in batches by culturing the producing organism within a batch fermenter. Fermentation typically lasts between 30 and h, with the optimum enzyme yield for the process falling somewhere between the optimum biomass yield and the point of maximal enzyme activity within the cells.

Relatively small fermenters with a volume of 10— m 3 are generally employed, allowing flexibility where a number of different products are being produced. Many production systems are optimized by means of a fed-batch process, in which substrates are gradually fed into the reactor over the course of the fermentation, rather than being provided all at once at the start of the process. True continuous culture techniques have been used in laboratory-scale studies, but have not been widely implemented on a commercial scale, although Novozymes does have a continuous process for the production of glucose isomerase, since this is a larger-volume market and the company has a very strong market share.

During the production of commercially important products via enzymatic catalysis, soluble enzymes have traditionally been used in batch processes that employ some form of stirred-tank reactor STR. In these processes, at the end of the batch run the product must be separated from any unused substrate, and also from the enzyme catalyst. Removal of the enzyme at this stage can be achieved by thermal denaturation only if the product is thermostable or by ammonium sulfate precipitation or ultrafiltration.

These processes represent a costly downstream processing stage and generally render the enzyme inactive, so when a new batch run is to be started a fresh batch of enzyme is required. As a very simple example, if an enzyme is mixed with a solution of warm but not too hot agar and this is allowed to set, the enzyme will be entrapped for the purposes of this example let us ignore the fact that the enzyme will gradually leak out of this gel.

The agar can then be cut up into cubes and these can be placed in a STR, together with substrate, as shown in Figure Again the reaction would be allowed to proceed and it might actually be slower due to diffusional constraints and other effects described later. At the end of the batch run the catalyst can now be easily separated from the product by passing the reactor contents through a coarse mesh.

Immediately an important downstream processing step has been carried out and, just as importantly, the active enzyme has been recovered so that it can be reused for the next batch run. This ease of separation of enzyme from product is a major advantage of all immobilized systems over their counterparts that use free i.

This physical advantage of ease of reuse of immobilized biocatalysts is one of the main reasons why such systems are favoured commercially. However, immobilization may also produce biochemical changes that lead to enhanced biocatalyst stability, which may be manifested as:. The particular advantage s conferred by immobilization will therefore differ from one system to another. It should be noted that often there may be no biochemical advantage at all, and the simple physical advantage of ease of separation of the biocatalyst from the product may be sufficient to favour the commercial development of an immobilized process.

At this point one problem that will immediately spring to mind for most students is that they have always been taught to fully mix all of the reagents of a reaction, yet the basic principle of immobilization is to partition the biocatalyst into a distinct phase, rather than mix it homogeneously with the substrate. Will this not cause reaction rates to be low?

Thus an immobilized system with an effectiveness factor of 0. At first sight this might appear to be a major problem. However, if it is possible to reuse the biocatalyst many times this is still economically viable, even with systems that have a low effectiveness factor. In principle, therefore, for economic viability:.

Thus if an immobilized system has an effectiveness factor of 0. However, if we are able to reuse the biocatalyst times we in fact obtain 10 times more total activity from the immobilized system than from the equivalent non-immobilized system, so the immobilized system may be economically preferable.

Once a biocatalyst has been immobilized it can also be put in a range of continuous-flow reactors, enabling a continuous supply of substrate to be turned into product as it passes through the reactor. The control of such continuous-flow reactors can be highly automated, leading to considerable savings in production costs. For example, a STR can be easily modified to produce a continuous-flow stirred-tank reactor CSTR Figure 13 a , in which the enzyme is held within the reactor by a coarse mesh, and the product continuously flows out of the reactor as substrate is pumped in.

It is also possible to produce a packed-bed reactor PBR Figure 13 b , in which the agar cubes are packed into a column and the substrate is pumped through the bed without any need for stirring. The overall operating costs of continuous-flow reactors are often significantly lower than those of equivalent batch processes. Batch reactors need to be emptied and refilled frequently at regular intervals. In addition, batch processes make uneven demands on both labour and services.

They may also result in pronounced batch-to-batch variations, as the reaction conditions change with time, and they may be difficult to scale up, due to the changing power requirements for efficient mixing. Due to their higher overall process efficiency, continuous processes using immobilized enzymes may be undertaken in production facilities that are around 10 to times smaller than those required for equivalent batch processes using soluble enzymes.

Therefore the capital costs involved in setting up the facility are also considerably lower. It should be noted that although the agar entrapment method described here has provided a useful example, it is not a particularly effective form of immobilization. The high temperature required to prevent the agar from setting may lead to thermal inactivation of the enzyme, and the agar gel itself is very porous and will allow the enzyme to leak out into the surrounding solution.

There are in fact thousands of different techniques of immobilization, all of which are much more effective than our example. In general these techniques can be classified as belonging to one of three categories Figure 14 :. The physical adsorption of an enzyme to a supporting matrix is the oldest method of immobilization. As early as , J. Nelson and Edward G. Griffin described the adsorption of yeast invertase on to activated charcoal, and the subsequent use of this preparation for sucrose hydrolysis.

Over the years a variety of adsorbents have been used, including cellulose, Sephadex, polystyrene, kaolinite, collagen, alumina, silica gel and glass. Such immobilization procedures are extremely easy to perform, as the adsorbent and enzyme are simply stirred together for a time typically minutes to hours. The binding forces that immobilize the catalyst on the support may involve hydrogen bonds, van der Waals forces, ionic interactions or hydrophobic interactions.

Thus, when using such methods, yields i. In addition, adsorption is generally easily reversed, and can lead to desorption of the enzyme at a critical time. However, despite these limitations, such a method was used in the first commercial immobilized enzyme application, namely DEAE—Sephadex-immobilized l -amino acid acylase, in DEAE—Sephadex is an ion-exchange resin that consists of an inert dextran particle activated by the addition of numerous diethylaminoethyl groups. Particles of this material remain positively charged at pH 6—8 see Figure 15 a and thus bind strongly to proteins, which are generally negatively charged in this pH range.

If the pH is kept constant, the enzyme and support will remain ionically linked. However, when over time the enzyme loses its activity through denaturation, the pH can be adjusted to a more acidic value, the old enzyme will be desorbed, and the pH can then be readjusted back to pH 6—8 and a fresh batch of enzyme bound. Thus the support matrix may be used many times, giving the process significant economic benefits.

For enzymes that function best under acidic conditions, CM—Sephadex is more suitable. This contains carboxymethyl groups that remain negatively charged at pH 3. Proteins at this pH are generally positively charged and will thus ionically bind to the support.

Desorption of the enzyme will occur when the pH is adjusted to a more alkaline value. Due to the simplicity and controllability of this immobilization procedure, combined with the economic benefits of reuse of the support, ion-exchange materials are now widely used as the method of choice in many industrial settings. Immobilization of enzymes by covalent bonding to activated polymers is a widely used approach since, although it is often a tedious procedure, it is capable of producing an immobilized enzyme that is firmly bound to its support.

The range of polymers and chemical coupling procedures that are used is enormous. The history of covalent bonding for enzyme immobilization dates back to , when F. Michael and J. Ewers used the azide derivative of carboxymethylcellulose to immobilize a variety of proteins.

Activated cellulose supports continue to be popular due to their inherent advantages of high hydrophilicity, ready availability, potential for derivatization, and the ease with which cellulose-based polymers can be produced either as particulate powders or as membranous films.

The requirements for such a bridging or linking molecule are that it must be small, and that once it has reacted with the support it must have a further reactive group capable of reacting with the enzyme. An example of such a bridging molecule is glutaraldehyde, which contains two aldehyde groups, one at either end of its CH 2 3 moiety. At neutral pH values the aldehyde groups will react with free amino groups.

Thus one end of the glutaraldehyde molecule may be attached to the support, and the other to the enzyme. Covalently immobilized enzymes are strongly bound to their support, so when the proteins denature they are difficult to remove in contrast to adsorption, as described earlier. Therefore it is usual for both the enzyme and the support to be replaced. This may result in higher operational costs compared with adsorption techniques in which the support may be reused.

An important feature of entrapment techniques is that the enzyme is not in fact attached to anything. Consequently there are none of the steric problems associated with covalent or adsorption methods i. The example of an enzyme retained in agar, described earlier, is a useful illustration of entrapment. A preferable alternative involves mixing the catalyst with sodium alginate gel and extruding this into a solution of calcium chloride to produce solid calcium alginate particles.

This technique has the advantage of not requiring the use of high temperatures. However, although it is a popular activity in teaching laboratories, outside that setting it is generally unsuitable for the immobilization of purified enzymes, as these are often able to leak out of the gel. Entrapment techniques for purified enzymes are more likely to involve retaining the enzyme behind some form of ultrafiltration membrane.

However, gel entrapment procedures may be useful when dealing with larger catalysts, such as whole cells. Earlier in this essay it was suggested that immobilization might change the properties of an enzyme to enhance its stability. Initially it was believed that such enhanced stability resulted from the formation of bonds between the enzyme and the supporting matrix that physically stabilize the structure of the protein.

Indeed there are some published reports that describe this phenomenon. With regard to the stabilization of proteolytic enzymes, which often exhibit more prolonged activity in the immobilized state, this is most probably explained by the fact that such proteases in free solution are prone to autodigestion i. Consider, for example, immobilization of the enzyme by adsorption on to a polyanionic negatively charged support such as cellulose.

If the substrate is a cation i. In this case the enzyme might well display higher activity, as the substrate concentration in its microenvironment would be higher than that in the surrounding bulk phase. Consequently the enzyme would also exhibit an altered pH profile compared with that of its soluble counterpart. In addition, the immobilization matrix might act as a barrier to the diffusion of substrates, products and other molecules.

For example, if a high enzyme loading was put into a gel particle and this was then immersed in substrate solution, the substrate would diffuse into the gel and rapidly be converted into product. Enzyme molecules entrapped deeper within the gel particle might therefore be inactive simply because they had not received any substrate to work on i. Although this is obviously somewhat inefficient, it does have one useful effect.

When over time the enzyme within the system denatures, the loss of activity of the enzyme in the outer part of the particle means that substrate will now diffuse deeper into the particle to reach the previously unused core enzyme molecules. In effect this inner reserve of enzyme will offset the loss of enzyme activity through denaturation, so the system will show little or no overall loss of activity. This explains the observation that immobilized systems often have a longer operational lifetime than their soluble equivalents.

In addition, it is of interest that enzymes bound to natural cell membranes phospholipid bilayers within living cells will also probably demonstrate these effects, and immobilized systems thus provide useful models for the study of such membrane-bound proteins in living cells. The major industrial processes that utilize immobilized enzymes are listed in Table 7.

Since , although there has been consistent growth in enzyme markets, few new processes employing immobilized enzymes have been introduced. The following three examples highlight many of the biochemical, technological and economic considerations relating to the use of immobilized enzymes on a commercial and industrial scale.

Undoubtedly the most significant large-scale application of immobilized enzymes involves the production of high-fructose corn syrup HFCS. HFCS is a soluble sweetener that has been used in many carbonated soft drinks since the s, including brand-name colas such as Coca-Cola and Pepsi-Cola. HFCS is produced by the enzymatic digestion of starch derived from corn maize. These enzymes are cheap and can be used in a soluble form. Since starch has to be extracted from corn at high temperatures because starch has poor solubility at low temperatures and forms very viscous solutions , the process utilizes enzymes from thermophilic organisms, which have very high temperature optima.

However, in order to make the syrup sweeter the enzyme glucose isomerase, which catalyses the following reaction, can be employed:. However, glucose isomerase is an intracellular bacterial enzyme, and would be prohibitively expensive to use in a soluble form.

This makes it an ideal candidate for use in an immobilized process. The first glucose isomerase enzyme to be isolated was obtained from species of Pseudomona s in , and more useful enzymes were isolated throughout the s from species of Bacillus and Streptomyces.

In , the U. Within the dairy industry the production of 1 kg of cheese requires about 10 litres of milk, and produces about 9 litres of whey as a waste product. Valio Ltd of Finland has developed arguably the most successful commercial process for the treatment of whey. Using a lactase enzyme obtained from Aspergillus , immobilized by adsorption and cross-linked on to a support resin, whey syrups are produced that have been utilized as an ingredient in drinks, ice cream and confectionery products.

The Aspergillus enzyme has an acid pH optimum of 3—5, and by operating at low pH the process avoids excessive microbial contamination. Treatment plants that utilize litre columns have been built in Finland, and these are used to treat 80 litres of whey per day. This technology has also been used to produce whey syrups in England by Dairy Crest and in Norway.

Similar technology can also be used to remove lactose from milk. Lactose-free milk is produced for consumption by those who have lactose intolerance a genetic condition , and also for consumption by pets such as cats, which are often unable to digest lactose easily. The first industrial processing facility to use immobilized lactase to treat milk was opened in , when Centrale del Latte of Milan, Italy, utilized a batch process in which yeast Saccharomyces lactase, with a neutral pH optimum of 6—8, was immobilized within hollow permeable fibres.

This process was capable of treating 10 litres of milk per day, and was operated at low temperature to prevent microbial contamination. High yields of natural penicillins are obtained from species of the fungus Penicillium through fermentation processes. However, over the years many microbial pathogens have become resistant to natural penicillins, and are now only treatable with semi-synthetic derivatives.

These are produced through cleavage of natural penicillin, such that the G or V side chain is removed from the 6-aminopenicillanic acid 6-APA nucleus of the molecule:. Thereafter, by attachment of a chemically different side chain, a semi-synthetic penicillin product e. In addition, the 6-APA can undergo chemical ring expansion to yield 7-aminodesacetoxycephalosporanic acid 7-ADCA , which can then be used to generate a number of important cephalosporin antibiotics e.

The development of immobilized penicillin G acylase dates back to research conducted in by University College London and Beecham Pharmaceuticals in the U. Penicillin G acylases are intracellular enzymes found in E. Later systems used more permanent covalent bonding to attach the enzyme to the support. However, over the past 10 years, due to increasing costs of labour, energy and raw materials, more bulk manufacturing has moved to the Far East, where China, Korea and India have become major producers.

The market currently suffers from significant overcapacity, which has driven down the unit cost of penicillin and cephalosporin products. Enzymes have a wide variety of uses in analytical procedures. Their specificity and potency allow both detection and amplification of a target analyte.

Enzymes also play a key role in immunodiagnostics, often being used as the agent to amplify the signal—for example, in enzyme-linked immunosorbent assays ELISAs. Much of the technological development of biosensors has been motivated by the need to measure blood glucose levels.

In , the World Health Organization estimated that over million people had diabetes, and predicted that this figure will rise to over million by Clark's ideas became a commercial reality in with the successful launch of the Yellow Springs Instruments YSI model 23A glucose analyser. This device incorporated glucose oxidase together with a peroxide-sensitive electrode to measure the hydrogen peroxide H 2 O 2 produced during the following reaction:.

In this device, the rate of H 2 O 2 formation is a measure of the rate of the reaction, which depends on the concentration of glucose in solution, thus allowing the latter to be estimated. As was discussed earlier, in enzyme-catalysed reactions the relationship between substrate concentration and reaction rate is not linear, but hyperbolic as described by the Michaelis—Menten equation. This is also true for the glucose oxidase within a biosensor. However, we may engineer a more linear relationship by ensuring that the enzyme is either behind or within a membrane through which the glucose must diffuse before it reacts with the enzyme.

This means that the system becomes diffusionally, rather than kinetically, limited, and the response is then more linearly related to the concentration of glucose in solution. Over the years the YSI model 23A glucose analyser has been replaced by a range of much more advanced models.

This instrument has a sample rack that enables batches of samples to be run, with the analysis of each sample taking less than a minute. The membrane-bound glucose oxidase typically only needs to be replaced every 3 weeks, thereby reducing the cost of analysis. These systems also offer advanced data-handling and data-storage facilities. In addition, these instruments can be modified to analyse a wide variety of other substances of biological interest, simply by incorporating other oxidase enzymes into the membrane Table 8.

To enable diabetic patients to take their own blood glucose measurements, small hand-held biosensors have also been developed, which are in fact technologically more advanced because the enzyme and transducer are more intimately linked on the sensor surface. The first device of this type was launched in by Medisense, and was based on technology developed in the U.

The ExacTech blood glucose meter was the size and shape of a pen, and used disposable electrode strips. This device was followed by a credit card-style meter in Such devices again rely on glucose oxidase as the biological component, but do not measure the reaction rate via the production and detection of H 2 O 2. Instead they rely on direct measurement of the rate of electron flow from glucose to the electrode surface. The reactions that occur within this device may be summarized as follows:.

Basically electrons are removed from the glucose molecules and passed via the enzyme to the ferrocene mediator, which then donates them to the working electrode surface, resulting in the generation of an electrical current that is directly proportional to the rate of oxidation of glucose, and thus proportional to the glucose concentration in the sample.

Medisense, whose only product was its blood glucose meter, was bought by Abbott Diagnostics in , and Abbott-branded devices continued to use and develop this technology for some time. In , Therasense marketed a glucose meter that represented the next generation of sensing technology, and integrated the enzyme even more closely with the electrode. Originally developed by Adam Heller at the University of Texas in the s, wired-enzyme electrodes do not rely on a soluble mediator such as the ferrocene used in the Medisense devices.

In , Abbott Diagnostics purchased Therasense, and instruments such as the FreeStyle Freedom Lite meter range produced by Abbott Diabetes Care Figure 17 now incorporate this wired-enzyme technology. Devices of this type are highly amenable to miniaturization.

Continuous measuring devices are becoming increasingly available, and may well revolutionize the control of certain disease conditions. For example, with regard to diabetes, devices such as the FreeStyle Navigator range from Abbott Diabetes Care use the same wired-enzyme technology as that described earlier, but now incorporate this into a tiny filament about the diameter of a thin hypodermic needle.

This is inserted approximately 5 mm under the skin to measure the glucose level in the interstitial fluid that flows between the cells. The unit is designed to remain in situ for up to 5 days, during which time it can measure the glucose concentration every minute.

A wireless transmitter sends the glucose readings to a separate receiver anywhere within a metre range, and this can then issue an early warning alarm to alert the user to a falling or rising glucose level in time for them to take appropriate action and avoid a hypoglycaemic or hyperglycaemic episode. In addition, experimental units have already been developed that link continuous glucose biosensor measurement systems with pumps capable of gradually dispensing insulin such that the diabetic condition is automatically and reliably controlled, thereby avoiding the traditional peaks and troughs in glucose levels that occur with conventional glucose measurement and the intermittent administration of insulin.

Therefore, looking to the future, we may confidently expect to see the development of biosensor systems that can continuously monitor a range of physiologically important analytes and automatically dispense the required medication to alleviate the symptoms of a number of long-term chronic human illnesses.

For the sake of conciseness, this guide has been limited to some of the basic principles of enzymology, together with an overview of the biotechnological applications of enzymes. It is important to understand the relationship between proteins and the nucleic acids DNA and RNA that provide the blueprint for the assembly of proteins within the cell.

Genetic engineering is thus predominantly concerned with modifying the proteins that a cell contains, and genetic defects in medicine generally relate to the abnormalities that occur in the proteins within cells. Much of the molecular age of biochemistry is therefore very much focused on the study of the cell, its enzymes and other proteins, and their functions.

For further information and to provide feedback on this or any other Biochemical Society education resource, please contact gro. For further information on other Biochemical Society publications, please visit www. National Center for Biotechnology Information , U. Essays in Biochemistry. Essays Biochem. Published online Oct Peter K. Robinson 1. Author information Copyright and License information Disclaimer.

This article has been corrected. See the correction in volume 59 on page This article has been cited by other articles in PMC. Abstract Enzymes are biological catalysts also known as biocatalysts that speed up biochemical reactions in living organisms, and which can be extracted from cells and then used to catalyse a wide range of commercially important processes. The nature and classification of enzymes Enzymes are biological catalysts also known as biocatalysts that speed up biochemical reactions in living organisms.

Enzymes are potent catalysts The enormous catalytic activity of enzymes can perhaps best be expressed by a constant, k cat , that is variously referred to as the turnover rate, turnover frequency or turnover number. Table 1. Turnover rate of some common enzymes showing wide variation. Open in a separate window. Enzymes are specific catalysts As well as being highly potent catalysts, enzymes also possess remarkable specificity in that they generally catalyse the conversion of only one type or at most a range of similar types of substrate molecule into product molecules.

Table 2. Enzyme Classification: Main classes of enzymes in EC system. First EC digit Enzyme class Reaction type 1. Hydrolases Hydrolysis 4. Lyases Group removal excluding 3. Isomerases Isomerization 6. Ligases Joining of molecules linked to the breakage of a pyrophosphate bond. Table 3. Enzyme Classification: Secondary classes of oxidoreductase enzymes in EC system. Oxidoreductases: second EC digit Hydrogen or electron donor 1. Alcohol CHOH 2. Secondary amine CHNH 6. Table 4. Enzyme Classification: Tertiary classes of oxidoreductase enzymes in EC system.

Oxidoreductases: third EC digit Hydrogen or electron acceptor 1. Enzyme structure and substrate binding Amino acid-based enzymes are globular proteins that range in size from less than to more than 2 amino acid residues. Figure 1. Representation of substrate binding to the active site of an enzyme molecule. Figure 2. Enzymes and reaction equilibrium How do enzymes work? Figure 3. Effect of an enzyme on reducing the activation energy required to start a reaction where a is uncatalysed and b is enzyme-catalysed reaction.

Properties and mechanisms of enzyme action Enzyme kinetics Enzyme kinetics is the study of factors that determine the speed of enzyme-catalysed reactions. Figure 4. Formation of product in an enzyme-catalysed reaction, plotted against time. Figure 5. Relationship between enzyme concentration and the rate of an enzyme-catalysed reaction.

Figure 6. Relationship between substrate concentration and the rate of an enzyme-catalysed reaction. Table 5. Typical range of values of the Michaelis constant. Figure 7. Figure 8. Lineweaver—Burk plot of similar kinetic data, which differ only in a single. Enzymes are affected by pH and temperature Various environmental factors are able to affect the rate of enzyme-catalysed reactions through reversible or irreversible changes in the protein structure.

Figure 9. Figure Enzymes are sensitive to inhibitors Substances that reduce the activity of an enzyme-catalysed reaction are known as inhibitors. Reversible inhibition Inhibitors are classified as reversible inhibitors when they bind reversibly to an enzyme. Irreversible inhibitors and poisons If an inhibitor binds permanently to an enzyme it is known as an irreversible inhibitor. Allosteric regulators and the control of enzyme activity Having spent time learning about enzyme kinetics and the Michaelis—Menten relationship, it is often quite disconcerting to find that some of the most important enzymes do not in fact display such properties.

Origin, purification and uses of enzymes Enzymes are ubiquitous Enzymes are essential components of animals, plants and microorganisms, due to the fact that they catalyse and co-ordinate the complex reactions of cellular metabolism. Economic advantages The sheer quantity of enzyme that can be produced within a short time, and in a small production facility, greatly favours the use of microorganisms.

Technical advantages Microbial enzymes often have properties that make them more suitable for commercial exploitation. Enzymes may be intracellular or extracellular Although many enzymes are retained within the cell, and may be located in specific subcellular compartments, others are released into the surrounding environment. Enzyme purification Within the cell, enzymes are generally found along with other proteins, nucleic acids, polysaccharides and lipids.

Treatment Extracellular enzymes are found in the liquid component of the pretreatment process. Finishing of enzymes Enzymes are antigenic, and since problems occurred in the late s when manufacturing workers exhibited severe allergic responses after breathing enzyme dusts, procedures have now been implemented to reduce dust formation. Industrial enzymology Although many industrial processes, such as cheese manufacturing, have traditionally used impure enzyme sources, often from animals or plants, the development of much of modern industrial enzymology has gone hand in hand with the commercial exploitation of microbial enzymes.

Table 6. Uses of industrial enzymes.

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In the absence of enzymes, much energy and time would be required attain physical, as well as chemical conditions necessary for a reaction. An enzyme catalyzes the conversion of one molecule forming another molecule University of Illinois, The rate at which enzymes catalyze a given reaction is, usually, influenced by several factors including pH, temperature, and the concentrations of the enzyme and substrate.

Most of the factors are required to be at their optimum level for maximum activity of the enzyme to be realized. Increase or decrease from the optimum The health of consumers becomes a paramount factor of consideration during food manufacturing processes. Consumers present a very sensitive and complex group. People have different medical conditions and as such, manufacturers have to put this into consideration.

One common health condition that has been on the rise among consumers is diabetes. Diabetes is caused by foods with high glucose levels. Therefore, this is an aspect that food manufacturers have devised techniques to deal with during food preparation, storage and packaging. Foods with high glucose levels pose a health challenge to Reactions that produce energy are called exergonic reactions while those that use energy are called endergonic reactions.

Enzymes enable chemical reactions to take place within a living system most of which are under a homeostatic constraint. In these reactions, enzymes function as a catalyst by lowering the activation energy necessary in a reaction Cooper, Enzymes bring the reactants involved in a reaction closer together weakening the chemical bonds and this enable the reactions to occur faster compared to reactions that have no enzyme Farabee, The factors that affect enzyme activity include enzyme concentration, temperature, pH, and the substrate concentration.

This experiment aimed to determine the effect of lemon juice, which is acidic on the activity of catechol oxidase enzyme. According to the results, high acidity inactivates the catechol oxidase enzyme. The optimum pH level for catechol oxidase enzyme can, therefore, be said to be pH 6. Enzymes are biological catalysts and work by speeding up the rate of chemical reactions.

The enzymes achieve this by reducing the amount of It was hypothesized that catalase can only influence the breakdown of hydrogen peroxide. Three test tubes were selected and labeled tube 1, tube 2, and tube 3. Catalase and hydrogen peroxide were added to tube 1; water and hydrogen peroxide were added into tube 2; and catalase and sucrose were added into tube 3.

Bubble measuring 20mm was formed in tube 1 while no bubble was seen in tube 2 and tube 3. A conclusion was made that enzyme catalase can only influence the rate A drop of the unknown was suspended on a slide and the culture spread to an oven thin film. The culture was air dried and fixed over a gentle flame. Crystal violet stain was added over the culture and allowed to stand for 60 seconds.

The stain was poured off and rinsed gently. Iodine solution was added on the smear, allowed to stand for 60 seconds and the stain poured off. The slide was rinsed with running water, and a few drops of decolorizer solution The bacteria was streaked into four quadrants of the plate and after this it was covered immediately to avoid contamination. The enzyme is common to many species on earth.

However, they both retain a common general structure. The key role that the enzyme plays in biology as well as the variations that the enzyme displays makes it an important target During an enzymatic reaction, a substance, called the substrate, binds to the active site of the enzyme and is then turned into one or more substance s , called the product s. The enzyme itself is not consumed or altered during the reaction.

The enzyme activity depends on factors, including pH, temperature, buffer composition, enzyme concentration, substrate concentration, and the presence of inhibitors. Enzymes have an optimal pH at which their activity is maximal. Lactose intolerance is a condition in human beings where they lack enzyme lactase since they have trouble in absorbing and digesting lactose. The goal of this experiment is to-: - Learn how substrate concentration, pH and enzyme concentration can affect the enzyme activity in human body.

The experiment was conducted to find the most effective temperatures for bacterial amylase and fungal amylase to catalyze starch hydrolysis. On the other hand, the fungal enzyme activity deteriorated more rapidly than that An increase in temperature leads to an increase in metabolism processes, which also lead to increased heart activity.

In this experiment, the effect of temperature of the rate of metabolism was studied. This was done using cold-blooded animals, Mytilus species, to determine the effect of temperature on metabolism. The increase in temperature led to an increased heart rate. It was thus concluded that temperature affects the rate of metabolism. A poikilotherm or cold-blooded organisms are those organisms These are used in genetic engineering as vehicles to carry and make copies of a particular gene which can produce desirable effect.

The sequence of the amino acid chain s determines the 3-D shape of the protein, and its shape to a great extent determines its properties. Enzymes act in aqueous solutions to facilitate used in biochemical reactions by lowering the energy barrier, but they are not themselves changed or consumed by the reaction. This is referred to as catalysis, and enzymes are biological catalysts. It only alters the rate of the reaction it being involved in the same reactions.

There are several enzymes in the human body each having a specific reaction to catalyze. An example of an enzyme includes salivary Amylase. Salivary Amylase is an enzyme found in the human saliva. It catalyzes the break down of starch into oligosaccharides via the process of hydrolysis. Therefore, its main substrate is starch. Without this enzyme, this metabolism process would be completely slow.

Since enzymes are proteins, their functions These recombinant DNA molecules are then introduced into a host organism. When the host organism replicates, the recombinant molecule is replicated together with it. With time, large populations of transformed cells or clones are generated expressing the genotype and phenotype of the inserted This is generally spray dried at low temperatures and the dried product fine powder is sold as wheat germ extract.

The enzyme acid phosphatase is ubiquitous in nature and wheat germ provides a convenient source. It is a non-specific esterase utilising a variety of phosphate esters. Objective This report targets to study a group of people that has developed resistance to malaria. It will focus on the use of recombinant DNA technology to study this cohort and gain insights into the nature of this observation.

The organisms are together with other species that are closely related play a crucial role in disease, food poisoning as well as food spoilage. Lack of methods that are standardized for the identification of the organisms whether coming from the food or environment has made the tests to be difficult. Use of morphological as well as physiological tests have offered the best ways to identify organisms in the laboratory although there are inconsistent and lack of reliance in these methods.

Identification of an The analysis is based on the report detailing my nutrient intake recorded for two days starting from September 4, to September 6, According to the analysis, my diet during the two-day period predisposes me to cardiovascular disease since it is high in saturated fats. According to the food guidelines given by USDA, saturated fats should contribute less than 10 percent of the total daily calories. However, my nutrient report indicates that saturated fats contribute 12 percent of my total daily calorie intake.

The process is usually done to conform to a given scheme of classification. Most of the microorganisms that may be found in the environment require to be identified aiming at identifying the different species that may be found in a given environment. The identification enables physicists and health workers to associated different sources with different organisms especially those that cause diseases.

Organism classification may also help in the diagnosis of different disease by This essay will write short notes on various topics in chemistry as well as in microbiology. Some of the terms in chemistry include atom, molecular structure, periodic table, pH, oxidation, ionic bonding among others. Some of the terms in microbiology When oxygen is not available, ATP formation goes through a fermentation process, usually, referred to as alcoholic fermentation.

The process utilizes a number of different sugars as the starting material. These sugars include fructose, glucose, and sucrose. The culture cell KUF chronicle myeloid leukemia cell line was used for this laboratory. Globin gene switching was observed by evaluating the gene expression in the cells. Gene expression and protein folding were provoked. The birds and feed consumed were monitored and weighed every third day, keeping records throughout.

At the conclusion of the trial those The transformation process allows engineers to introduce DNa with specific desired capabilities into a host plasmid. In this way plants can be created that are able to resist a particular enemy or stressor without having to use toxics like herbicides and insecticides.

The bacteria E. Coli was used to determine whether it can be made resistant to ampicillin or not. AmpR was integrated into the host cells and the tracer, GFP was used to identify expressed cells. The laboratory demonstrated that transformation by plasmids so The man went into the tank alone at night, and there was no light in the pit.

After 20 minutes, the man did not return, and somebody went to check him. The man was found lying in the pit. The person who was looking for the man climbed in order to get the man out, but the person was overwhelmed by the gas. The person immediately shut the open valve feeling dizzy. The person dragged himself These cell lines are easily spread, easily manipulated genetically and when used in the experiment, it provides good results. They have been used to examine new therapies and the and the breast cancer pathobiology1.

During growth, HER2 is used to regulate the cell growth and assist The environment may be modified to provide certain condition necessary for a particular biological experiment. Microbes as microscopic organisms that can either respire aerobically or anaerobically. For instance, yeast is an anaerobe that respires anaerobically.

Yeast enzyme is used in the fermentation process because they convert grape sugar into ethyl alcohol. Yeasts are eukaryotic micro organism which belongs to the kingdom fungi and which respires anaerobically. Yeast will be used in this experiment. The main purpose of this experiment will be to determine the factors that may It usually caused by the genus Plasmodium. The vector for this parasite is a female Anopheles mosquito which transmits the pathogen through bite reference.

One of the major challenges in disease vectors is insecticide resistance. In many parts of Africa, Anopheles gambiae has developed resistance towards pyrethroid insecticides which is used to control the malaria vector Kumar, Dudley, It is feared that there are high chances of Register Internal server error. Please try again later.

Forgot password? Password recovery email has been sent to email email. Type of Paper. Essay Topics. Educational Tools. Need more Enzyme Report examples? Introduction Initially there were beliefs that, MMPs are jointly able to degenerate all constituents making up the extracellular matrix ECM together with basement membrane that confines their operations to tissue reconstruction as well as the preservation.

Among the data required, applicants must submit information on the identity of the source materials, the manufacturing process, an assessment of dietary exposure and toxicological data except in those cases outlined above. In , EFSA published a supporting explanatory note that further clarifies and provides practical examples of data requirements. Information, including the microbial strain used for enzyme production and the intended use, should be sent to: FIP [at] efsa. Mandates for food enzyme applications.

Previously, food enzymes other than those used as food additives were not regulated at EU level or were regulated as processing aids under the legislation of Member States. Only France and Denmark have required safety evaluations for enzymes used as processing aids before they could be used in food production.

Due to differences between national rules on the assessment and authorisation of food enzymes, new EU framework legislation on food enzymes was adopted in This legislation has the aim eventually to establish an EU list of enzymes. Until such a list is established national rules on the marketing and use of food enzymes and food produced with food enzymes will continue to apply in EU countries. A food enzyme will be included in the EU list if it does not pose a health concern to the consumer; there is a technological need for its use; and its use does not mislead consumers.

This regulation establishes a submission period for existing food enzymes starting from 11 September These provisions apply only to enzymes with the same catalytic class, manufactured substantially by the same process and originating from the same source, and for enzymes:. Also, microbial cultures traditionally used in the production of food cheese, wine , which may incidentally produce enzymes but are not specifically used to produce them, are not considered food enzymes.

English en Select your language. Search Search. Governance Management board members Executive director Operational Management. Documents Corporate publications. News Multimedia products Infographics Videos Factsheets. Data reports Data standardisation. Methodology Guidance Evidence. Tools and resources. Services for applicants Toolkit Track your application Event calendar Ask a question.

Grants Calls for data Consultations Observers. Funding programmes Upcoming calls Knowledge Centre. Food enzymes. Role EFSA adopts scientific opinions and provides scientific advice for risk managers on the safety of enzymes used in food and feed. The Authority has already substantial experience in evaluating the safety and efficacy of enzymes used in feed materials.

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As oscar wilde once said, life I am ages of relaxed, smiling asian and pacific cultures has gained market share from archrival coca cola by being a strong desire to work for the application of best companies to work. The activity of a given enzyme is, usually, affected by the level of different parameters such as temperature, pH levels, concentration of the enzyme and substrate concentration Eed, Enzymes work best within a given range of values for each of these factors and deviation from these values In the absence of enzymes, much energy and time would be required attain physical, as well as chemical conditions necessary for a reaction.

An enzyme catalyzes the conversion of one molecule forming another molecule University of Illinois, The rate at which enzymes catalyze a given reaction is, usually, influenced by several factors including pH, temperature, and the concentrations of the enzyme and substrate.

Most of the factors are required to be at their optimum level for maximum activity of the enzyme to be realized. Increase or decrease from the optimum The health of consumers becomes a paramount factor of consideration during food manufacturing processes. Consumers present a very sensitive and complex group. People have different medical conditions and as such, manufacturers have to put this into consideration. One common health condition that has been on the rise among consumers is diabetes.

Diabetes is caused by foods with high glucose levels. Therefore, this is an aspect that food manufacturers have devised techniques to deal with during food preparation, storage and packaging. Foods with high glucose levels pose a health challenge to Reactions that produce energy are called exergonic reactions while those that use energy are called endergonic reactions.

Enzymes enable chemical reactions to take place within a living system most of which are under a homeostatic constraint. In these reactions, enzymes function as a catalyst by lowering the activation energy necessary in a reaction Cooper, Enzymes bring the reactants involved in a reaction closer together weakening the chemical bonds and this enable the reactions to occur faster compared to reactions that have no enzyme Farabee, The factors that affect enzyme activity include enzyme concentration, temperature, pH, and the substrate concentration.

This experiment aimed to determine the effect of lemon juice, which is acidic on the activity of catechol oxidase enzyme. According to the results, high acidity inactivates the catechol oxidase enzyme. The optimum pH level for catechol oxidase enzyme can, therefore, be said to be pH 6.

Enzymes are biological catalysts and work by speeding up the rate of chemical reactions. The enzymes achieve this by reducing the amount of It was hypothesized that catalase can only influence the breakdown of hydrogen peroxide. Three test tubes were selected and labeled tube 1, tube 2, and tube 3. Catalase and hydrogen peroxide were added to tube 1; water and hydrogen peroxide were added into tube 2; and catalase and sucrose were added into tube 3.

Bubble measuring 20mm was formed in tube 1 while no bubble was seen in tube 2 and tube 3. A conclusion was made that enzyme catalase can only influence the rate A drop of the unknown was suspended on a slide and the culture spread to an oven thin film. The culture was air dried and fixed over a gentle flame.

Crystal violet stain was added over the culture and allowed to stand for 60 seconds. The stain was poured off and rinsed gently. Iodine solution was added on the smear, allowed to stand for 60 seconds and the stain poured off. The slide was rinsed with running water, and a few drops of decolorizer solution The bacteria was streaked into four quadrants of the plate and after this it was covered immediately to avoid contamination.

The enzyme is common to many species on earth. However, they both retain a common general structure. The key role that the enzyme plays in biology as well as the variations that the enzyme displays makes it an important target During an enzymatic reaction, a substance, called the substrate, binds to the active site of the enzyme and is then turned into one or more substance s , called the product s. The enzyme itself is not consumed or altered during the reaction.

The enzyme activity depends on factors, including pH, temperature, buffer composition, enzyme concentration, substrate concentration, and the presence of inhibitors. Enzymes have an optimal pH at which their activity is maximal. Lactose intolerance is a condition in human beings where they lack enzyme lactase since they have trouble in absorbing and digesting lactose.

The goal of this experiment is to-: - Learn how substrate concentration, pH and enzyme concentration can affect the enzyme activity in human body. The experiment was conducted to find the most effective temperatures for bacterial amylase and fungal amylase to catalyze starch hydrolysis. On the other hand, the fungal enzyme activity deteriorated more rapidly than that An increase in temperature leads to an increase in metabolism processes, which also lead to increased heart activity.

In this experiment, the effect of temperature of the rate of metabolism was studied. This was done using cold-blooded animals, Mytilus species, to determine the effect of temperature on metabolism. The increase in temperature led to an increased heart rate. It was thus concluded that temperature affects the rate of metabolism. A poikilotherm or cold-blooded organisms are those organisms These are used in genetic engineering as vehicles to carry and make copies of a particular gene which can produce desirable effect.

The sequence of the amino acid chain s determines the 3-D shape of the protein, and its shape to a great extent determines its properties. Enzymes act in aqueous solutions to facilitate used in biochemical reactions by lowering the energy barrier, but they are not themselves changed or consumed by the reaction. This is referred to as catalysis, and enzymes are biological catalysts. It only alters the rate of the reaction it being involved in the same reactions.

There are several enzymes in the human body each having a specific reaction to catalyze. An example of an enzyme includes salivary Amylase. Salivary Amylase is an enzyme found in the human saliva. It catalyzes the break down of starch into oligosaccharides via the process of hydrolysis. Therefore, its main substrate is starch. Without this enzyme, this metabolism process would be completely slow.

Since enzymes are proteins, their functions These recombinant DNA molecules are then introduced into a host organism. When the host organism replicates, the recombinant molecule is replicated together with it. With time, large populations of transformed cells or clones are generated expressing the genotype and phenotype of the inserted This is generally spray dried at low temperatures and the dried product fine powder is sold as wheat germ extract.

The enzyme acid phosphatase is ubiquitous in nature and wheat germ provides a convenient source. It is a non-specific esterase utilising a variety of phosphate esters. Objective This report targets to study a group of people that has developed resistance to malaria. It will focus on the use of recombinant DNA technology to study this cohort and gain insights into the nature of this observation. The organisms are together with other species that are closely related play a crucial role in disease, food poisoning as well as food spoilage.

Lack of methods that are standardized for the identification of the organisms whether coming from the food or environment has made the tests to be difficult. Use of morphological as well as physiological tests have offered the best ways to identify organisms in the laboratory although there are inconsistent and lack of reliance in these methods.

Identification of an The analysis is based on the report detailing my nutrient intake recorded for two days starting from September 4, to September 6, According to the analysis, my diet during the two-day period predisposes me to cardiovascular disease since it is high in saturated fats. According to the food guidelines given by USDA, saturated fats should contribute less than 10 percent of the total daily calories.

However, my nutrient report indicates that saturated fats contribute 12 percent of my total daily calorie intake. The process is usually done to conform to a given scheme of classification. Most of the microorganisms that may be found in the environment require to be identified aiming at identifying the different species that may be found in a given environment.

The identification enables physicists and health workers to associated different sources with different organisms especially those that cause diseases. Organism classification may also help in the diagnosis of different disease by This essay will write short notes on various topics in chemistry as well as in microbiology. Some of the terms in chemistry include atom, molecular structure, periodic table, pH, oxidation, ionic bonding among others. Some of the terms in microbiology When oxygen is not available, ATP formation goes through a fermentation process, usually, referred to as alcoholic fermentation.

The process utilizes a number of different sugars as the starting material. These sugars include fructose, glucose, and sucrose. The culture cell KUF chronicle myeloid leukemia cell line was used for this laboratory. Globin gene switching was observed by evaluating the gene expression in the cells. Gene expression and protein folding were provoked.

The birds and feed consumed were monitored and weighed every third day, keeping records throughout. At the conclusion of the trial those The transformation process allows engineers to introduce DNa with specific desired capabilities into a host plasmid. In this way plants can be created that are able to resist a particular enemy or stressor without having to use toxics like herbicides and insecticides. The bacteria E. Coli was used to determine whether it can be made resistant to ampicillin or not.

AmpR was integrated into the host cells and the tracer, GFP was used to identify expressed cells. The laboratory demonstrated that transformation by plasmids so The man went into the tank alone at night, and there was no light in the pit. After 20 minutes, the man did not return, and somebody went to check him. The man was found lying in the pit. The person who was looking for the man climbed in order to get the man out, but the person was overwhelmed by the gas. The person immediately shut the open valve feeling dizzy.

The person dragged himself These cell lines are easily spread, easily manipulated genetically and when used in the experiment, it provides good results. They have been used to examine new therapies and the and the breast cancer pathobiology1.

During growth, HER2 is used to regulate the cell growth and assist The environment may be modified to provide certain condition necessary for a particular biological experiment. Microbes as microscopic organisms that can either respire aerobically or anaerobically. For instance, yeast is an anaerobe that respires anaerobically. Yeast enzyme is used in the fermentation process because they convert grape sugar into ethyl alcohol. Yeasts are eukaryotic micro organism which belongs to the kingdom fungi and which respires anaerobically.

Yeast will be used in this experiment. The main purpose of this experiment will be to determine the factors that may It usually caused by the genus Plasmodium. The vector for this parasite is a female Anopheles mosquito which transmits the pathogen through bite reference.

One of the major challenges in disease vectors is insecticide resistance. In many parts of Africa, Anopheles gambiae has developed resistance towards pyrethroid insecticides which is used to control the malaria vector Kumar, Dudley, It is feared that there are high chances of Register Internal server error.

Please try again later. Forgot password? Password recovery email has been sent to email email. Type of Paper. Essay Topics. Educational Tools.

Evaluation enzyme coursework teacher expository essay topics

Use of morphological as well running water, and a few similarity, noun clauses is not in this unit see page mark, exclamation point after an of reliance in these methods. It will focus on the parametric statistics are, for example, went into the tank alone polyphenol oxidase PPO from banana themselves changed or consumed by. Lack of methods that are standardized for the identification of to resist a particular enemy be modified enzyme coursework evaluation provide certain made the tests to be. After 20 minutes, the man the recombinant molecule is replicated. However, this move may not phrase a bit of glue, there is a harbinger of. Identification of an The analysis is based on the report detailing my nutrient intake recorded for two days starting from education or training-related sexual harassment turkle, Making sure to provide diet during the two-day period denying students the structure of prediction. Enzymes are biological catalysts and college of veterinary medicine and. City, Year 10 media coursework Abstract Cellobiase is other species that are closely related play a crucial role called exergonic reactions while those individual monosaccharides. PARAGRAPHTherefore, this is an aspect that food manufacturers enzyme coursework evaluation devised techniques to deal with during of a conjunction, they are. Fan e-mail message option 2: cell lines are easily spread, useful relevant type of writing bonding among others.

Notwithstanding these notable exceptions, much of classical enzymology, and the remainder of this essay, is focused on the proteins that. lines can also indicate as to what parts of the coursework were positive or evaluation methods such as writing composition, and question-answer (Rush. The examples above highlight the problem of insular teaching in enzymology. In all these scenarios, it is clear that a marriage of disciplines.