Modern Enzymes And Its Effect On The Field Of Genetics And Protein Engineering

In this lab or experiment, the aim was to determine the following factors of enzymes: (1) the effects of enzymes concentration the catalytic rate or the rate of the reaction, (2) the effects of pH on a particular enzyme, an enzyme known and referred throughout this experiment as ALP (alkaline phosphate enzyme) and lastly (3) the effects of various temperatures on the reaction or catalytic rate. Throughout the experiment 8 separate cuvettes and tubes are mixed with various solutions (labeled as tables 1,3 & 4 in the apparatus/materials sections of the lab) and tested for the effects of the factors mentioned above (concentration, pH and temperature). The tubes labeled 1-4 are tested for pH with pH paper and by spectrophotometer, cuvettes 1a-4a was tested for concentration and cuvettes labeled 1b-4b was tested for temperature in four different atmospheric conditions (4ºC, 23ºC, 32ºC and 60ºC) to see how the enzyme solution was affected by the various conditions. After carrying out the procedures the results showed that the experiment followed the theory for the most part, which is that all the factors work best at its optimum level. So, the optimum pH that the enzymes reacted at was a pH of 7 (neutral), the optimum temperature that the reactions occurs with the enzymes is a temperature of 4ºC or

The use of multiple test tubes and Parafilm was used for each experiment. Catechol, potato juice, pH 7 phosphate buffer, and stock potato extract 1:1 will be used to conduct the following experiments: temperature effect on enzyme activity, the effect of pH on enzyme action, the effect of enzyme concentration, and the effect of substrate concentration on enzyme activity. For the temperature effect on enzyme activity, three test tube were filled with three ml of pH 7 phosphate buffer and each test tube was labels 1.5 degrees Celsius, 20 °C, and 60 °C. The first test tube was placed in an ice-water bath, the second test tube was left at room temperature, and the third test tube was placed in approximately 60°C of warm water. After filling the test tubes with three ml of the

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

Introduction:Enzymes are made up of proteins which are produced within living cells and act as catalysts which speed up chemical reactions. They are made up of long chains of amino acids containing carbon, hydrogen, oxygen and nitrogen. Enzymes are structured to be

These results shown from this experiment led us to conclude that enzymes work best at certain pH rates. For this particular enzyme, pH 7 worked best. When compared to high levels of pH, the lower levels worked better. The wrong level of pH can denature enzymes; therefore finding the right level is essential. The independent variable was the amount of pH, and the dependent being the rate of oxygen. The results are reliable as they are reinforced by the fact that enzymes typically work best at neutral pH

Background and Introduction: Enzymes are proteins that process substrates, which is the chemical molecule that enzymes work on to make products. Enzyme purpose is to increase the rate of activity and speed up chemical reaction in a form of biological catalysts. The enzymes specialize in lowering the activation energy to start the process. Enzymes are very specific in their process, each substrate is designed to fit with a specific substrate and the enzyme and substrate link at the active site. The binding of a substrate to the active site of an enzyme is a very specific interaction. Active sites are clefts or grooves on the surface of an enzyme, usually composed of amino acids from different parts of the polypeptide chain that are brought together in the tertiary structure of the folded protein. Substrates initially bind to the active site by noncovalent interactions, including hydrogen bonds, ionic bonds, and hydrophobic interactions. Once a substrate is bound to the active site of an enzyme, multiple mechanisms can accelerate its conversion to the product of the reaction. But sometimes, these enzymes fail or succeed to increase the rate of action because of various factors that limit the action. These factors can be known as temperature, acidity levels (pH), enzyme and/or substrate concentration, etc. In this experiment, it will be tested how much of an effect

Enzymes are an organic substance that are made up of polymers of amino acids that help the digestive system and metabolic processes in living organisms (Funk and Wagnalls, 2016). Enzymes are able

Enzymes are a key aspect in our everyday life and are a key to sustaining life. They are biological catalysts that help speed up the rate of reactions. They do this by lowering the activation energy of chemical reactions (Biology Department, 2011).

Introduction: Enzymes are protein catalysts facilitating the conversion of substrates into products (Alexander and Peters, 2011). They go through a whole chemical reaction which starts off with the substrate and then ends up with a product. The only way this reaction can be adjusted or not even work is if they end up going through some sort of affect which only temperature and pH levels can do determining the environment. When enzymes are in an environment that is too acidic or alkaline, their chemical properties, sizes and shapes can become altered (Magher, 2015) Chemical modification of proteins is widely used as a too; to maintain a native conformation, improving stability (Rodriguez-Cabrera, Regalado, and Garcia-Almendarez, 2011) In this experiment, four trials were conducted and recorded every 15 seconds for 5 minutes in order to calculate the optimum levels and IRV.

“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].

Organisms cannot depend solely on spontaneous reactions for the production of materials because they occur slowly and are not responsive to the organism's needs (Martineau, Dean, et al, Laboratory Manual, 43). In order to speed up the reaction process, cells use enzymes as biological catalysts. Enzymes are able to speed up the reaction through lowering activation energy. Additionally, enzymes facilitate reactions without being consumed (manual,43). Each enzyme acts on a specific molecule or set of molecules referred to as the enzyme's substrate and the results of this reaction are called products (manual 43). As a result, enzymes promote a reaction so that substrates are converted into products on a faster pace (manual 43). Most enzymes are proteins whose structure is determined by its sequence of its amino acids. Enzymes are designed to function the best under physiological conditions of PH and temperature. Any change of these variables that change the conformation of the enzyme will destroy or enhance enzyme activity(manual, 43).

The purpose of this lab report is to investigate the effect of substrate concentration on enzyme activity as tested with the enzyme catalase and the substrate hydrogen peroxide at several concentrations to produce oxygen. It was assumed that an increase in hydrogen peroxide concentration would decrease the amount of time the paper circle with the enzyme catalase present on it, sowing an increase in enzyme activity. Therefore it can be hypothesised that there would be an effect on catalase activity from the increase in hydrogen peroxide concentration measured in time for the paper circle to ride to the top of the solution.

In recent years, the biotechnological use of xylans and xylanases has grown remarkably (Aristidou and Pentillä 2000; Subramaniyan and Prema 2002; Beg et al., 2001; Techapun et al., 2003). The end-products of xylan degradation of considerable importance in commercial applications are furfural and xylitol (Parajó et al., 1998). Xylan can be converted to β-D-xylopyranosyl and its oligosaccharides via two types of hydrolysis: acid or enzymatic. Acid hydrolysis is often preferred because it is faster, but it is accompanied by the formation of toxic compounds that may hinder subsequent microbial fermentation. Furthermore, in the long run, it can lead to corrosion of the metallic equipment that comes in contact with the acid. Recently, some industrial companies have shown interest in the development of efficient enzymatic processes to be used instead of acid hydrolysis in the treatment of material containing hemicellulose. Commercial xylanases are industrially produced, for example, in Japan, Finland, Germany, Republic of Ireland, Denmark, Canada and the USA. The microorganisms used to obtain these enzymes are Aspergillus niger, Trichoderma sp. and Humicola insolens. Nevertheless, commercial xylanases can also be obtained from bacteria. Xylanase began to be used in the 1980s: initially in the preparation of animal feed and later in the food, textile and paper industries. Currently, xylanase and cellulase, together with pectinases, account for 20% of the world enzyme market.

Once we identify a list of candidate enzymes that are predicted to be compatible with the crystal lattice. The first step would be to check viability of the crystals in the reaction buffers and temperatures compatible with each of the enzymes. To test this, we will again use the strand displacement

The enhancement in the production of cellulases enzymes is another strategy being attempted consistently for reducing the cost of the cellulases. The use of the low cost renewable substrates can significantly reduce the cost of enzyme production. The lignocellulosic biomass could be used as a raw material for enzyme production (Klein-Marcuschamer et al., 2012; Ellila et al., 2017). The cellulases are inducible enzymes (Acharaya and Chaudhry, 2012). Many of the current commercial cellulases production technologies rely on fungal microorganisms and expression of cell wall degrading enzymes in the filamentous fungi is best induced in the presence of insoluble lignocellulosic substrates (Znameroski et al., 2012; Sohail et al., 2016). Also this has been proposed that enzyme complexes perform best on lignocellulose hydrolysis when the same substrate is used for their production (Sukumaran et al., 2005). The submerged fermentation (SmF) is the most widely used technology for the production of cellulases commercially. However, the problems of longer fermentation times and