The Effects Of Salt Stress On Protein Metabolism

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

The role of an enzyme is to catalyse reactions within a cell. The enzyme present in a potato (Solanum Tuberosum) is catechol oxidase. In this experiment, the enzyme activity was tested under different temperature and pH conditions. The objective of this experiment was to determine the ideal conditions under which catechol oxidase catalyses reactions. In order to do this, catechol was catalyzed by catechol oxidase into benzoquinone at diverse temperatures and pH values. The enzyme was exposed to its new environment for 5 minutes before the absorbance of the catechol oxidase was measured at 420 nm using a spectrophotometer. The use of a spectrophotometer was crucial for the collection of data in this experiment. When exposed to hot and cold temperatures, some enzymes were found to denature causing the activity to decrease. Similarly, when the pH was too high or low, then the catechol oxidase enzyme experienced a significant decrease in activity. It can be concluded after completing this experiment that the optimal pH for catechol oxidase is 7 and that the prime temperature is 20º C. Due to the fact that the catechol oxidase was only tested under several different temperatures and pH values, it is always possible to get a more precise result by decreasing the increments between the test values. However, our experiment was able to produce accurate results as to the

vulgaris plants, via the formation of a standard curve prepared using varying concentrations of bovine serum albumin (BSA) solution. Following absorbance readings of the various BSA solutions, they were plotted against their concentrations providing an indirect measure for determining protein concentrations of the plant samples within the assay tubes, and through further calculations the sample protein concentration. The mean protein concentration for the control group was calculated to be 3.34 ± 1.30 mg/mL, while the mean treated group concentration was 2.01 ± 1.26 mg/mL. These results similarly like the chlorophyll results correlate with the literature articles, as a reduced protein content within the Paraquat treated plants can be expected to some extent (Chia et al., 1981). This reduction in protein concentration is the result of those superoxide anions produced by Paraquat, disrupting the chloroplast membranes and allowing for intracellular components including some proteins to leak out, hence the decrease in protein concentration in comparison to the non-treated plants (Qian et al., 2009). A slight outlier may exist within the treated groups protein concentrations as one of the groups provided a negative value for protein concentration which is not valid, but even after exclusion of that data value, results are still supportive of the expected outcome. Though these results support the claim of Paraquat toxicity causing membrane deterioration and leakiness, protein concentration values are rather more purposeful when used to analyze malondialdehyde (MDA) values on per mg of protein

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

Rubisco is the most abundant protein on earth that is essential for carbon fixation in plants. For the protein to function at its optimal level, it needs to be isolated from the mixture of proteins and in its purest form. The three isolation techniques carried out in this lab are salting out, ion exchange chromatography, and SDS-PAGE. Rubisco will be purer as each technique is conducted and will be in its purest form after the last isolation technique is carried out.

The aim of my investigation is to see how pH affects the activity of potato tissue catalase, during the decomposition of hydrogen peroxide to produce water and oxygen.

This experiment demonstrates the effects of pH on the rate of photosynthesis by examining the behavior of leaf disks in different pH solutions under light. In this experiment, we used five different pH levels: pH 5, pH 6, pH 7, pH 8 and pH 9. These solutions were created using a combination of hydrochloric acid and sodium hydroxide. Spinancia olcerea or spinach, leaves were used in the experiment to examine the effects of pH on the rate of photosynthesis. The rate of photosynthesis was measured by counting the number of leaf disks that rose to the surface of the solution after each minute. In acidic solutions, the rate of photosynthesis increased while in basic solutions, the rate of photosynthesis decreased.

Based on the class data of the pH of phosphorylase reaction, the potato phosphorylase is reached the endpoint which the phosphorylase active at pH 6, it started active within 6 minutes. The optimal pH of phosphorylase is at pH 7 which active just within 4 minutes. At pH 6, it started to breaking down the starch primer +glucose-1-phosphase into starch + phosphate which reacted with the iodine test to formed the blue precipitate. At the optimal pH 7, it shows that it maximized its activity. Comparing the data of the pH of the potato phosphorylase reaction with the study published by Russell Pressey from Plant

Enzymes are high molecular weight molecules and are proteins in nature. Enzymes work as catalysts in biochemical reactions in living organisms. Enzyme Catecholase is found on in plants, animals as well as fungi and is responsible for the darkening of different fruits. In most cases enzymatic activities are influenced by a number of factors, among them is temperature, PH, enzyme concentration as well as substrate concentration (Silverthorn, 2004). In this experiment enzyme catecholase was used to investigate the effects of PH and enzyme concentration on it rate of reaction. A pH buffer was used to control the PH, potato juice was used as the substrate and water was used as a solvent.

In the following experiments we will measure precise amounts of potato extract as well as Phenylthiourea, combined with or without deionized water and in some instances change the temperature and observe and record the reaction. We will also investigate the different levels of prepared pH on varying samples of the potato extract and the Phenylthiourea and record the results. We will answer question such as what is the best temperature for optimum temperature reaction as well as the best pH level for the same reaction.

To study the effects of hypotonic, hypertonic and isotonic solutions on plant and animal cells.

The Effects that 1%, 4%, and 16% Sodium Chloride (NaCl) Concentration Had on the Rate of Reaction of Catecholase Enzymes in a Potato (Solanum tuberosum).

Water and light are two of many essential needs responsible for a range of plant processes ensuring the growth and survival of plants. (Johnson, 2011) Water is crucial as it is used during photosynthesis, to dissolve nutrients, to help with the regulation of temperature and as a transporter for food and minerals. Nutrients that are absorbed by the plant through active transport (which can be defined as the movement of a substance across the membrane going against the concentration gradient, from low concentration to high concentration) include nitrogen, potassium, phosphorous, sulfur and magnesium. All of which are macronutrient ions meaning they exist as ions in the soil, and then are absorbed when they are dissolved in water. Each one of

The cell wall plasma membrane (CWPs) interface is believed as a key site for the HM stress signal perception. The CWPs involved in response to various abiotic stresses, have been extensively identified and characterised in different crop plants. Under various stress conditions, the main CWPs include phospholipases, the salt overly sensitive kinases, transcription factors, C-repeat binding factor, dehydration sensitive element binding proteins, mitogen activated proteins kinases and phosphatases, and abscisic acid responsive element binding factors (Ihsan et al., 2017; Dar et al., 2017). There are known CW proteins which forms covalent bonds and undergo glycosylation with HMs some

Figure 2: Proteoid roots produced by white lupin with (A) and without (B) phosphate.: proteoid roots of P-sufficient plants, marked as proteoid (+P); lateral roots of P-sufficient plants, marked as lateral (+P); active proteoid roots of P-deficient plants, marked as proteoid (-P); lateral roots of P-deficient plants, marked as lateral (-P). (Adapted from: Watt and Evans, 1999).