A lipase enzyme has been isolated from a bacterium with a strong red color, found in industrial waste from a fishing company. This enzyme has great potential for elaboration of degreasers for industrial use as it can work at a wide range of temperature (between 4 ° and 80 ° C). However, it is estimated that its purity for industrial purposes is only 35% since it is contaminated with a low molecular weight protein that binds the smallest red pigment peptides and salts product of the purification process 1- Propose a methodology to increase the degree of purity of this enzyme, eliminating small proteins and color. 2- How it is ensured that the degree of purity of the enzyme has increase

A lipase enzyme has been isolated from a bacterium with a strong red color, found in industrial waste from a fishing company. This enzyme has great potential for elaboration of degreasers for industrial use as it can work at a wide range of temperature (between 4 ° and 80 ° C). However, it is estimated that its purity for industrial purposes is only 35% since it is contaminated with a low molecular weight protein that binds the smallest red pigment peptides and salts product of the purification process 1- Propose a methodology to increase the degree of purity of this enzyme, eliminating small proteins and color. 2- How it is ensured that the degree of purity of the enzyme has increase

Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter10: From Proteins To Phenotypes

Section: Chapter Questions

Problem 10QP: b. Compounds A, B, C, and D are known to be intermediates in the pathway for production of protein...

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a. Compounds A, B, C, and D are known to be intermediates in the pathway for production of protein E. To determine where the block in protein-E production occurred in each individual, the various intermediates were given to each individuals cel Is in culture. After a few weeks of growth with the intermediate, the cells were assayed for the production of protein E. The results for each individuals cells are given in the following table. A plus sign means that protein E was produced after the cells were given the intermediate listed at the top of the column. A minus sign means that the cells still could not produce protein E even after being exposed to the intermediate at the top of the column. Draw the pathway leading to the production of protein E.
. You need to prepare 500 μL of a 250 µg/mL bovine gamma globulin solution, for one of your protein standards in the Bradford assay. The available bovine gamma globulin in the lab is in the form of a 2 mg/mL stock solution, and it can be diluted with deionized water. Describe or show below how you would create your desired 250 µg/mL solution.
Compounds A, B, C, and D are known to be intermediates in the pathway for production of protein E. To determine where the block in protein-E production occurred in each individual, the various intermediates were given to each individual’s cell in culture. After a few weeks of growth with the intermediate, the cells were assayed for the production of protein E. The results for each individual’s cells are given in the following table. A plus sign means that the protein E was produced after the cells were given the intermediate listed at the top of the column. A minus sign means that the cells still could not produce protein E even after being exposed to the intermediate at the top of the column. a) If an individual who is homozygous for the mutation found in individual 2 and heterozygous for the mutation found in individual 4 mates with an individual who is homozygous for the mutation found in individual 4 and heterozygous for the mutation found in individual 2, what could the…
Upon doing the experiment of Protein Denaturation, what could be observed in the precipitation of heavy metal ions if an albumin solution in a solution is dropped with drops of silver nitrate and then it will be shaken? Explain.
Consider the following properties of the protein components of a sample mixture as provided in the table below: 1. if the mixture is subjected to gel filtration chromotography which protein component elute first? 2. if the mixture is subjected to isoelectric focusing which protein will stop m oving nearest to the positive electrode? 3. if the mixture is subjected to cation-exchange chromotography using a buffer at ph 7 which protein will bind to the resin? 4.if the mixture is subjected to SDS-PAGE which protein will be at bottomost portion of gel? 5.if the mixture is subjected to hydrophobic interaction chromotography which protein will bind most strongly to the resin?
The OXA-M290 protein is next purified by size exclusion chromatography. To determine the best type of size exclusion resin to use, the size of OXA-M290 must first be determined. Earlier, you determined the amino acid sequence of OXA-M290 (MRVLALSAVFLVASIIGMPAVAKEWQENKSWNAHFTEHKSQGVVVLWNENKQQGFTNNLKRANQAFLPASSAKIPNSLIALDLGVVKDEHQVFKWDGQTRDIATWNRDHNLITAMKYSVVPVYQEFARQIGEARMSKMLHAFDYGNEDISGNVDSFWLDGGIRISATEQISFLRKLYHNKLHVSERSQRIVKQAMLTEANGDYIIRAKTGYDTKIGWWVGWVELDDNVWFFAMNMDMPTSDGLGLRQAITKEVLKQEKIIP). Based on the amino acid sequence, what is the molecular weight of this protein? You can use the free ProtParam tool (https://web.expasy.org/protparam/) to calculate the molecular weights of proteins. Make sure to include units in your answer. Note: The amino acid sequence reported earlier does not include the His-tag that was added to OXA-M290 by the pET-28a vector. However, you do not need to consider the amino acids in the His-tag in your answer to this question. For Context ONLY: For…
In a mixed heteropolymer experiment, messages were createdwith either 4/5C:1/5A or 4/5A:1/5C. These messages yielded proteinswith the amino acid compositions shown in the followingtable. Using these data, predict the most specific coding compositionfor each amino acid.4/5C:1/5A 4/5A:1/5CPro 63.0% Pro 3.5%His 13.0% His 3.0%Thr 16.0% Thr 16.6%Glu 3.0% Glu 13.0%Asp 3.0% Asp 13.0%Lys 0.5% Lys 50.0% 98.5% 99.1%
In a paragraph form, provide the experimental procedures in removal of the carbon dioxide present in the mechanism of reaction of protein that contain native serine residues by the reaction of oxazetidine-containing peptides and α-ketoacid
The following data describe the catalysis of cleavage of peptide bonds in small peptides by the enzyme UTSAse (the arrow indicates the peptide bond cleaved in each case). Substrate Km(mM) kcat(s-1) PAPA↓G 4.0 26 PAPA↓A 1.5 37 PAPA↓F 0.64 18 what features of amino acid sequence dictate the specificity of the proteolytic cleavage? Large hydrophilic R-groups Large hydrophobic R-groups Neutral R-groups Small hydrophilic R-groups Large hydrophobic R-groups Negatively charged R-groups Positively charged R-groups
Most bacterial mutants that require isoleucine for growth also require valine.Why? Which enzyme or reaction would be defective in a mutant requiringonly isoleucine (not valine) for growth?
In the Biuret Assay for protein concentration determination, the role of sodium potassium tartrate is to prevent the (gaining, losing) of electrons by Cu2+.
When performing his experiments on protein refolding, Christian Anfinsen obtained a quite different result when reduced ribonuclease was reoxidized while it was still in 8 M urea and the preparation was then dialyzed to remove the urea. Ribonuclease reoxidized in this way had only 1% of the enzymatic activity of the native protein. Why were the outcomes so different when reduced ribonuclease was reoxidized in the presence and absence of urea?