Sigma Erdrich Lab

In this experiment, 4 grams of peeled turnip was used to prepare the enzyme extract opposed to the 1 gram of turnip suggested by Fundamentals of Life Science. Along with the change to the amount of turnip used, the amount of 0.1M phosphate buffer used to prepare the enzyme extract was changed from 50mL to 30mL. The affect of temperature on enzyme activity was not

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

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

* The beakers labelled; Solutions of lipase respectively at concentrations of 1%, 2%, 3%, and 4% were made using lipase at 5% and distilled water.

To prevent fluctuation in the pH, a solution known as a “buffer solution” was used in the experiment. Buffer solutions are mixtures of at least two chemicals which counteract the effect of acids and alkalis. Therefore, when a small quantity of alkali or acid solution is added the pH of the enzyme doesn’t change.

enzymes that will be used during this lab to test the ability of amylase to break down starch ,a

After the substrate solution was added, five drops of the enzyme were quickly placed in tubes 3, 4 and 5. There were no drops of enzyme added in tubes 1 and 2 and in tube 6 ten drops were added. Once the enzyme solution has been added the tubes were then left to incubate for ten minutes and after five drops of DNSA solution were added to tubes 1 to 6. The tubes were then placed in a hot block at 80-90oC for five minutes. They were then taken out after the five minute period and using a 5 ml pipette, 5 ml of distilled water were added to the 6 tubes and mixed by inversion. Once everything was complete the 6 tubes were then taken to the Milton Roy Company Spectronic 21 and the absorbance of each tube was tested.

This experiment is to study and measure the enzyme activity of β-galactosidase in the different concentrations of o-Nitrophenylgalactoside (ONPG) using a spectrophotometer. The spectrophotometer was also set at 420nm, a wavelength which is best for recording the absorbance values for the experiment. From the results, 0.9mM ONPG solution has the highest absorbance and 0.1mM ONPG solution has the least. Also, 0.5mM ONPG solution has the highest rate of enzyme activity and it is the most efficient as the enzyme activity of the ONPG solution continues even though the other concentrations of ONPG solution has already stopped the enzymatic reactions as the substrate is already used up.

In the exercise # 2 we observed the effect of substrate concentration, enzyme concentration, pH and temperature on enzyme activity. All the data showed that once potato extract was added to catechol and water the reaction varied dependent on the level of catechol. As in

Prevotella intermedia has a unique hemolytic activity. Proteases produced by Prevotella can destroy a number of proteins involving collagen and fibronectin. It has been shown that proteases possess trypsin-like properties that characterize mainly cysteine

Combination of aspergillopeptidase A and Aspergillus acid carboxypeptidase was efficient in deodorizing and debittering soybean protein hydrolysates(Article 2009). Alcalase treated wheat gluten hydrolysates had less bitterness level and overall acceptability of the product increased(Koo et al. 2014).

2. Introduction: Each student was given unknown bacteria and was instructed to perform a variety of experimental tests that would help to identify their bacteria. During the process of identification, the unknown bacteria was added to many different testing medias using aseptic technique. They are as follows: lactose fermentation on eosin methylene blue (EMB), TSI (Triple Sugar Iron agar), Phenol red sucrose, the SIM test, H2S by SIM, IMViC (indole, motility, voges-proskauer, and citrate), Urease (urea broth), PDase (Phenylalanine Deaminase), Lysine Decarboxylase, and Ornithine Decarboxylase. Colonial morphology on EMB was used to

Chitin (N-acetylglucosamine [GlcNAc]) content was analyzed as described [53, 54]. 5 mg of dried mycelia were resuspended in 1 ml of 6% KOH and were heated with 80℃ for 90 min. Samples were centrifuged (16,000×g, 10 min) and pellets were washed with PBS for three times (16,000 ×g,10 min) before final suspension in 0.5 ml of McIlvaine’s buffer (pH 6.0). An aliquot of 100 ml (13 units) of Streptomyces plicatus chitinase (Sigma) was added and was incubated for 16 h at 37℃ with gentle mixing. Samples (100 ml) were then combined with 100 ml of 0.27 M sodium borate (pH 9.0) and heated for 10 min at 100℃. Finally, 1 ml of freshly diluted (1:10) Ehrlich’s reagent (10 g β-dimethylaminobenzaldehyde in 1.25 ml of HCl and 8.75 ml of glacial acetic acid) was added. After being cooled down to room temperature, 200 μl of samples are added with 1 ml Ehrlich’s solution

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