By completing this experiment, knowledge collected about optimal pH in enzymes will help
1 “substrate” and another “ enzyme.” Instead of using the distilled water, this time you are going to use different pH buffer in the enzyme test tube. In the substrate tube, add 7 mL of distilled water, 0.3 mL of hydrogen peroxide, and 0.2 mL of guaiacol for a total volume of 7.5 mL. For the enzyme tube, instead of distilled water add the pH solution (3) and 1.5 mL of peroxidase which equals a total volume of 7.5 mL. Use the dH2O syringe for our pH solution. To clean the syringe, flush it by drawing 6 mL of distilled water.
Figure 20 and 21 casting tray Figure 22 gel box After 1 hr., take out the gel from gel box carefully, place it into the machine, so that the DNA gel electrophoresis can be visualize under UV light. Figure 23 gel documentation system, used to visualize gel electrophoresis with UV light NMR spectroscopy First of all, 3 samples were prepared, peptide in SDS, DPC, and buffer. The sample temperature was maintained at 298 K, prepared by supervisor and H(hydrogen) in SDS and DPC micelle was replaced with D(deuterium) , so that in proton NMR, peptide won’t be interfered by H in micelle. amount of peptide in sds and dpc
LABORATORY REPORT Activity: Enzyme Activity Name: Natalie Banc Instructor: Elizabeth Kraske Date: 09.26.2016 Predictions 1. Sucrase will have the greatest activity at pH 6 2. Sucrase will have the greatest activity at 50 °C (122 °F) 3.
LABORATORY REPORT Activity: Enzyme Activity Name: Natalie Banc Instructor: Elizabeth Kraske Date: 09.22.2016 Predictions 1. Sucrase will have the greatest activity at pH 6 2. Sucrase will have the greatest activity at 50 °C (122 °F) 3. Sucrase activity increases with increasing sucrose concentration Materials and Methods Effect of pH on Enzyme Activity 1. Dependent Variable amount of product (glucose and fructose) produced 2.
1.1 Abstract The purpose of quantitative analysis of protein using a spectrophotometer is to measure the concentration of proteins in a given sample. The experiment is conducted by laboratory method (Biuret Test) and using spectrophotometer to analyze the absorbance of reactants at 540 nm, hence determining the concentration of the proteins in a given sample. The purpose of stopped enzyme assay to study B-galactosidase is to determine the effect of temperature and concentrations of substrate on enzyme activity.
It is evident that there were errors present though out gel electrophoresis in terms of timing the traveling of the DNA and the photography of the gel. As mentioned before humans have between 2 – 20 copies of the gene, and that humans have at least 2 copies of every gene one maternally and one paternally. Seeing that the entire class only had one gene copy, it is evident that something must have been done incorrectly during the use of computer tools to find the Adj. Vol (INT) on a blurry image or something went wrong with the PCR mixture. Thus it is not possible to correlate the AMY1 gene copy number and the concentration of salivary amylase based on our results alone, so in the process we are also unable to disprove or prove the results obtained by the Parry
The enzymeʼs have an active site that allows only certain substances to bind, they do this by having an enzyme and substrate that fit together perfectly. If the enzyme shape is changed then the binding
Gastric juice has a low PH of 2, and most would think why don’t our internal organs get digested due to the acidic juice that resides in our stomachs? This does not happen, because of all the cells lining our stomachs, along with a protective layer of a muscle that contains mucus that shield the lining of our stomachs. Why Aren’t Organs Digested with Stomach Acid? Animals do not digest their own internal organs due to specialty cells that are within our stomachs, like serosa, mucosa also including parietal cells, gastrin cells (g-cells) and epithelial cells.
5 water bath were set up each to10 °C. (5 were used do the experiment faster) 5 cm3 of starch solution were added into the 5 test tubes that were labeled test tubes. Then 5 cm3 of amylase enzyme was added into the other 5 test tubes that were labeled. Put one of the starch solution test tube (preferably the one labeled 1) and one of the test tube containing amylase into the water bath (10 °C).
ABSTRACT: The purpose of the experiments for week 5 and week 6 support each other in the further understanding of enzyme reactions. During week 5, the effects of a substrate and enzyme concentration on enzyme reaction rate was observed. Week 6, the effects of temperature and inhibitor on a reaction rate were monitored. For testing the effects of concentrations, we needed to use the table that was used in week 3, Cells.
Usually, the microbial enzymes have various potential uses in industries and medicine. The microbial enzymes are also more reliable than plant and animal enzymes as they are more stable and active. Also the microorganisms demonstrate an alternative source of enzymes because they can be cultured in large quantities in a short time by fermentation and owing to their biochemical diversity and susceptibility to gene manipulation. Industries are looking for new microbial strains in order to produce different enzymes to fulfil the current enzyme
1.3.3 Methods of the measurement of DNase activity In 1950, the first method of the measurement of DNase I activity was described by Kunitz196. He isolated and precipitated DNase from fresh beef pancreas and isolated thymus nucleic acid. He found that the cleavage of DNA by crystalline DNase is accompanied by increase of absorption (at 260 nm) of UV light. This spectrophotometric method of measurement of the rate of the increase in the light absorption was then used for estimating of DNase activity. It lasted 43 years until in 1993 Nadano et al.
The gel was then soaked in GelRed for 20 minutes and examined under UV light. To prepare the digestions 10 μL of each digestion was mixed with 2 μL of 6X track dye in a micro centrifuge tube. 12 μL of 1 kb DNA ladder and each digestion was run on the
A direct current is passed through the gel, and it passes through electrodes at each end of the chamber. Since DNA is negatively charged, it will be attracted to the positive pole and repelled by the negative pole. Small DNA molecules are able to move through the gel faster than larger fragments. This results in a series of
